109l
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(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...)
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Revision as of 13:34, 29 October 2007
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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 ... [(full description)]
About this Structure
109L is a [Single protein] structure of sequence from [Coliphage t4] with CL and BME as [ligands]. Active as [[1]], 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
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