Sheets in Proteins - Revision history

Karsten Theis at 11:00, 6 August 2021

Karsten Theis — Fri, 06 Aug 2021 11:00:06 GMT

←Older revision		Revision as of 11:00, 6 August 2021
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	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='43/437754/1/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.		A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='43/437754/1/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.

-	~~Twisted~~ sheets ~~are~~ found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl/5'>domain 2</scene> of glycogen phosphorylase. An examples of <scene name='Sheets_in_Proteins/1dtg1/2'>antiparallel twisted sheet</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.	+	Real sheets (rather than the simple models shown above) as found in globular proteins are <scene name='43/437754/6ssc_antiparallel/1'>twisted</scene>. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl/5'>domain 2</scene> of glycogen phosphorylase. An examples of <scene name='Sheets_in_Proteins/1dtg1/2'>antiparallel twisted sheet</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.

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Karsten Theis: Beta strand moved to Sheets in Proteins over redirect: original title

Karsten Theis — Sat, 20 Jul 2019 20:16:47 GMT

Beta strand moved to Sheets in Proteins over redirect: original title

←Older revision

Revision as of 20:16, 20 July 2019

Karsten Theis: Sheets in Proteins moved to Beta strand: better search results

Karsten Theis — Sat, 20 Jul 2019 20:16:04 GMT

Sheets in Proteins moved to Beta strand: better search results

←Older revision

Revision as of 20:16, 20 July 2019

Eric Martz: /* Notes and References */

Eric Martz — Thu, 21 Jun 2018 22:09:54 GMT

Notes and References

←Older revision		Revision as of 22:09, 21 June 2018
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		+
		+	== See Also ==
		+	* [[User:Stephen Mills/Secondary Structure: Sheets]]
		+	* [[Secondary structure]]

	== Notes and References ==		== Notes and References ==
	<references/>		<references/>

Jaime Prilusky at 15:33, 21 June 2016

Jaime Prilusky — Tue, 21 Jun 2016 15:33:33 GMT

←Older revision		Revision as of 15:33, 21 June 2016
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	<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />		<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />
-	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='~~Sheets_in_Proteins~~/~~Syn_sheet7~~/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.	+	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='43/437754/1/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.

	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl/5'>domain 2</scene> of glycogen phosphorylase. An examples of <scene name='Sheets_in_Proteins/1dtg1/2'>antiparallel twisted sheet</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.		Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl/5'>domain 2</scene> of glycogen phosphorylase. An examples of <scene name='Sheets_in_Proteins/1dtg1/2'>antiparallel twisted sheet</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.

Karl Oberholser at 16:11, 21 June 2012

Karl Oberholser — Thu, 21 Jun 2012 16:11:27 GMT

←Older revision		Revision as of 16:11, 21 June 2012
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	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.		A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.

-	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl/5'>domain 2</scene> of glycogen phosphorylase. An examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel twisted sheet</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.	+	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl/5'>domain 2</scene> of glycogen phosphorylase. An examples of <scene name='Sheets_in_Proteins/1dtg1/2'>antiparallel twisted sheet</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.

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Karl Oberholser at 16:01, 21 June 2012

Karl Oberholser — Thu, 21 Jun 2012 16:01:00 GMT

←Older revision		Revision as of 16:01, 21 June 2012
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	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.		A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.

-	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/~~Gly_phosyl4~~/1'>domain 2</scene> of glycogen phosphorylase. ~~There are also~~ examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel ~~sheets~~</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.	+	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl/5'>domain 2</scene> of glycogen phosphorylase. An examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel twisted sheet</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.

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Karl Oberholser at 15:32, 15 June 2012

Karl Oberholser — Fri, 15 Jun 2012 15:32:18 GMT

←Older revision		Revision as of 15:32, 15 June 2012
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	<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />		<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />
-	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all ~~psi and~~ phi values to ~~135~~° and ~~-139~~°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.	+	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all phi and psi values to -139° and 135°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.

	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. There are also examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.		Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. There are also examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.

Karl Oberholser at 15:28, 15 June 2012

Karl Oberholser — Fri, 15 Jun 2012 15:28:41 GMT

←Older revision		Revision as of 15:28, 15 June 2012
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	<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />		<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />
-	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all psi and phi values to 135° and -139°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. ~~Psi~~ and ~~phi~~ values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of ~~+135~~° and ~~-139~~°, respectively. The median values for a parallel sheet are ~~+113~~° and ~~-119~~°.	+	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all psi and phi values to 135° and -139°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°.

-	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>~~psi and~~ phi values</scene> for randomly chosen residues. There are a wide range of values for both ~~psi and~~ phi, ~~+96~~° to ~~+148~~° and ~~-108~~° to ~~-142~~°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. There are also examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of ~~psi and~~ phi for randomly chosen residues; these values range from ~~+90~~° to ~~+167~~° and from ~~-98~~° to ~~-178~~°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for ~~psi and~~ phi are ~~+140~~° and ~~-125~~°, respectively.	+	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>phi and psi values</scene> for randomly chosen residues. There are a wide range of values for both phi and psi, -108° to -142° and +96° to +148°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. There are also examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of phi and psi for randomly chosen residues; these values range from -98° to -178° and from +90° to +167°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for phi and psi are -125° and +140°, respectively.

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Angel Herraez: fix some typos, insert degree symbols

Angel Herraez — Sun, 01 Apr 2012 18:12:26 GMT

fix some typos, insert degree symbols

←Older revision		Revision as of 18:12, 1 April 2012
Line 1:		Line 1:
	<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />		<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Structures of Sheets' scene='Sheets_in_Proteins/Syn_sheet1/2' />
-	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all psi and phi values to 135~~<sup>0</sup>~~ and -139~~<sup>0</sup>~~, respectively.</ref>. (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>) The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>~~hydrogne~~ bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Psi and phi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of +135~~<sup>0</sup>~~ and -139~~<sup>0</sup>~~, respectively. The median values for a parallel sheet are +113~~<sup>0</sup>~~ and -119~~<sup>0</sup>~~.	+	A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another as the one shown on the right<ref>This model was hand constructed using HyperChem and setting all psi and phi values to 135° and -139°, respectively.</ref> (<scene name='Sheets_in_Proteins/Syn_sheet1/2'> (Initial scene)</scene>). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/3'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. Another way of detecting the <scene name='Sheets_in_Proteins/Syn_sheet7/1'>antiparallel sheet</scene> is by displaying as cartoon. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet4/1'>hydrogen bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. These hydrogen bonds provide the major attractive force which maintains the sheet structure. Psi and phi values that permit this alignment in antiparallel sheets have <scene name='Sheets_in_Proteins/Syn_sheet5/1'>median values</scene> of +135° and -139°, respectively. The median values for a parallel sheet are +113° and -119°.

-	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>psi and phi values</scene> for randomly chosen residues. There are a wide range of values for both psi and phi, +96 to +148 and -108 to -142, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. ~~Examples~~ of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of psi and phi for randomly chosen residues; these values range from +90 to +167 and from -98 to -178, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for psi and phi are +140~~<sup>0</sup>~~ and -125~~<sup>0</sup>~~, respectively.	+	Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets, the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>psi and phi values</scene> for randomly chosen residues. There are a wide range of values for both psi and phi, +96° to +148° and -108° to -142°, respectively. The above sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. There are also examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. <scene name='Sheets_in_Proteins/1dtg4/3'> Values</scene> of psi and phi for randomly chosen residues; these values range from +90° to +167° and from -98° to -178°, respectively. These ranges overlap the values for the twisted parallel showing that there is no differences in the ranges for the two types of twisted sheets. Median values for psi and phi are +140° and -125°, respectively.

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