109l
From Proteopedia
(New page: 200px<br /> <applet load="109l" size="450" color="white" frame="true" align="right" spinBox="true" caption="109l, resolution 1.85Å" /> '''STRUCTURAL BASIS OF...) |
|||
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
| - | The propensity of an amino acid to form an alpha helix in a protein was, determined by multiple amino substitutions at positions 44 and 131 in T4, lysozyme. These positions are solvent-exposed sites within the alpha, helices that comprise, respectively, residues 39 to 50 and 126 to 134., Except for two acidic substitutions that may be involved in salt bridges, the changes in stability at the two sites agree well. The stability values, also agree with those observed for corresponding amino acid substitutions, in some model peptides. Thus, helix propensity values derived from model, peptides can be applicable to proteins. Among the 20 naturally occurring, amino acids, proline, glycine, and alanine each have a structurally unique, feature that helps to explain their low or high helix .. | + | The propensity of an amino acid to form an alpha helix in a protein was, determined by multiple amino substitutions at positions 44 and 131 in T4, lysozyme. These positions are solvent-exposed sites within the alpha, helices that comprise, respectively, residues 39 to 50 and 126 to 134., Except for two acidic substitutions that may be involved in salt bridges, the changes in stability at the two sites agree well. The stability values, also agree with those observed for corresponding amino acid substitutions, in some model peptides. Thus, helix propensity values derived from model, peptides can be applicable to proteins. Among the 20 naturally occurring, amino acids, proline, glycine, and alanine each have a structurally unique, feature that helps to explain their low or high helix propensities. For, the remaining 17 amino acids, it appears that the side chain hydrophobic, surface buried against the side of the helix contributes substantially to, alpha helix propensity. |
==About this Structure== | ==About this Structure== | ||
| - | 109L is a | + | 109L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] with CL and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=109L OCA]. |
==Reference== | ==Reference== | ||
Structural basis of amino acid alpha helix propensity., Blaber M, Zhang XJ, Matthews BW, Science. 1993 Jun 11;260(5114):1637-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8503008 8503008] | Structural basis of amino acid alpha helix propensity., Blaber M, Zhang XJ, Matthews BW, Science. 1993 Jun 11;260(5114):1637-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8503008 8503008] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t2]] |
| + | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blaber, M.]] | [[Category: Blaber, M.]] | ||
| Line 20: | Line 21: | ||
[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:50:09 2007'' |
Revision as of 13:43, 12 November 2007
|
STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
Overview
The propensity of an amino acid to form an alpha helix in a protein was, determined by multiple amino substitutions at positions 44 and 131 in T4, lysozyme. These positions are solvent-exposed sites within the alpha, helices that comprise, respectively, residues 39 to 50 and 126 to 134., Except for two acidic substitutions that may be involved in salt bridges, the changes in stability at the two sites agree well. The stability values, also agree with those observed for corresponding amino acid substitutions, in some model peptides. Thus, helix propensity values derived from model, peptides can be applicable to proteins. Among the 20 naturally occurring, amino acids, proline, glycine, and alanine each have a structurally unique, feature that helps to explain their low or high helix propensities. For, the remaining 17 amino acids, it appears that the side chain hydrophobic, surface buried against the side of the helix contributes substantially to, alpha helix propensity.
About this Structure
109L is a Single protein structure of sequence from Enterobacteria phage t2 with CL and BME as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Structural basis of amino acid alpha helix propensity., Blaber M, Zhang XJ, Matthews BW, Science. 1993 Jun 11;260(5114):1637-40. PMID:8503008
Page seeded by OCA on Mon Nov 12 15:50:09 2007
