Turns in Proteins
From Proteopedia
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<Structure load='1abb' size='500' frame='true' align='right' caption='' scene='Turns_in_Proteins/Hemery/1' /> | <Structure load='1abb' size='500' frame='true' align='right' caption='' scene='Turns_in_Proteins/Hemery/1' /> | ||
Since turns are classified as a type of secondary structure, they have an ordered, repetitive structure. There are about six different classes of β-turns with all of them containing four residues, but each class has a different range of psi and phi values for the second and third residues. Pro and Gly are commonly found in positions two and three, respectively, because their unique side chains permit a sharp bend in the peptide chain. A hydrogen bond formed between the backbond atoms of residues one and four is the major force maintaining the conformation of the bend in the chain, and in one class a Pro in the third position has the cis configuration which maintains the sharp bend without the aid of a hydrogen bond. | Since turns are classified as a type of secondary structure, they have an ordered, repetitive structure. There are about six different classes of β-turns with all of them containing four residues, but each class has a different range of psi and phi values for the second and third residues. Pro and Gly are commonly found in positions two and three, respectively, because their unique side chains permit a sharp bend in the peptide chain. A hydrogen bond formed between the backbond atoms of residues one and four is the major force maintaining the conformation of the bend in the chain, and in one class a Pro in the third position has the cis configuration which maintains the sharp bend without the aid of a hydrogen bond. | ||
| - | <scene name='Turns_in_Proteins/Gly_phosyl/ | + | |
| + | <scene name='Turns_in_Proteins/Gly_phosyl/3'>Domain 2</scene> chain a glycogen phosphorylase. | ||
<scene name='Turns_in_Proteins/Gly_phosyl_3turn/1'>glycogen phosporylase 3 turns</scene> | <scene name='Turns_in_Proteins/Gly_phosyl_3turn/1'>glycogen phosporylase 3 turns</scene> | ||
Revision as of 16:55, 2 March 2011
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Since turns are classified as a type of secondary structure, they have an ordered, repetitive structure. There are about six different classes of β-turns with all of them containing four residues, but each class has a different range of psi and phi values for the second and third residues. Pro and Gly are commonly found in positions two and three, respectively, because their unique side chains permit a sharp bend in the peptide chain. A hydrogen bond formed between the backbond atoms of residues one and four is the major force maintaining the conformation of the bend in the chain, and in one class a Pro in the third position has the cis configuration which maintains the sharp bend without the aid of a hydrogen bond.
chain a glycogen phosphorylase.
. of first turn.
