115l

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[[Image:115l.jpg|left|200px]]
[[Image:115l.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 115l |SIZE=350|CAPTION= <scene name='initialview01'>115l</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_115l", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_115l| PDB=115l | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=115l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=115l OCA], [http://www.ebi.ac.uk/pdbsum/115l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=115l RCSB]</span>
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}}
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'''STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME'''
'''STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME'''
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[[Category: Blaber, M.]]
[[Category: Blaber, M.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:26:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:26:54 2008''
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Revision as of 06:26, 2 May 2008

Image:115l.jpg

Template:STRUCTURE 115l

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

115L is a Single protein structure of sequence from Enterobacteria phage t4. 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 Fri May 2 09:26:42 2008

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