103l
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(New page: 200px<br /> <applet load="103l" size="450" color="white" frame="true" align="right" spinBox="true" caption="103l, resolution 1.9Å" /> '''HOW AMINO-ACID INSER...)
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Revision as of 13:33, 29 October 2007
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HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
Overview
Studies of extant protein sequences indicate that amino-acid insertions, and deletions are preferentially located in loop regions, which has, traditionally been explained as the result of selection removing, deleterious mutations within secondary structural elements from the, population. But there is no a priori reason to discount the possibility, that insertions within secondary structure could either be tolerated until, compensatory mutations arise, or have effects that are propagated away, from secondary structure into loops. Earlier studies have indicated that, insertions are generally tolerated, although much less well within, secondary structure elements than in loop regions. Here we show that, amino-acid insertions in an alpha-helix of T4 lysozyme can be accepted in, two different ... [(full description)]
About this Structure
103L is a [Single protein] structure of sequence from [Coliphage t4] with CL and BME as [ligands]. Full crystallographic information is available from [OCA].
Reference
How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme., Heinz DW, Baase WA, Dahlquist FW, Matthews BW, Nature. 1993 Feb 11;361(6412):561-4. PMID:8429913
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