1cv0: Difference between revisions

Revision as of 21:25, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1cv0.png

Template:STRUCTURE 1cv0

T4 LYSOZYME MUTANT F104MT4 LYSOZYME MUTANT F104M

Template:ABSTRACT PUBMED 10545167

About this StructureAbout this Structure

1CV0 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding., Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW, Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:10545167

Page seeded by OCA on Mon Jun 30 21:25:28 2008

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OCA

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-[[Image:1cv0.gif|left|200px]]
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 {{STRUCTURE_1cv0|  PDB=1cv0  |  SCENE=  }}
-'''T4 LYSOZYME MUTANT F104M'''
+===T4 LYSOZYME MUTANT F104M===
-==Overview==
+<!--
-In an attempt to identify a systematic relation between the structure of a protein and its folding kinetics, the rate of folding was determined for 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type residue (Leu, Ile, Phe, Val, or Met) was substituted with alanine. Methionine, which approximated the size of the original side chain but which is of different shape and flexibility, was also substituted at most of the same sites. Mutations that substantially destabilize the protein and are located in the carboxy-terminal domain generally slow the rate of folding. Destabilizing mutations in the amino-terminal domain, however, have little effect on the rate of folding. Mutations that have little effect on stability tend to have little effect on the rate, no matter where they are located. These results suggest that, at the rate-limiting step, elements of structure in the C-terminal domain are formed and have a structure similar to that of the fully folded protein. Consistent with this, two variants that somewhat increase the rate of folding (Phe104 --&gt; Met and Val149 --&gt; Met) are located within the carboxy-terminal domain and maintain or improve packing with very little perturbation of the wild-type structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_10545167}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10545167 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10545167}}
 ==About this Structure==
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 [[Category: Protein folding]]
 [[Category: T4 lysozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:08:18 2008''
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