216l
From Proteopedia
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| - | [[Image:216l.jpg|left|200px]] | + | [[Image:216l.jpg|left|200px]] |
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| - | '''STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME''' | + | {{Structure |
| + | |PDB= 216l |SIZE=350|CAPTION= <scene name='initialview01'>216l</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 216L is a [ | + | 216L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. This structure supersedes the now removed PDB entry 116L. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=216L 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:// | + | Structural basis of amino acid alpha helix propensity., Blaber M, Zhang XJ, Matthews BW, Science. 1993 Jun 11;260(5114):1637-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8503008 8503008] |
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:42:14 2008'' |
Revision as of 13:42, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
216L is a Single protein structure of sequence from Bacteriophage t4. This structure supersedes the now removed PDB entry 116L. 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 Thu Mar 20 15:42:14 2008
