2mea: Difference between revisions

Revision as of 16:16, 29 July 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:2mea.png

Template:STRUCTURE 2mea

CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONSCHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

Template:ABSTRACT PUBMED 10556244

About this StructureAbout this Structure

2MEA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme., Funahashi J, Takano K, Yamagata Y, Yutani K, Protein Eng. 1999 Oct;12(10):841-50. PMID:10556244

Page seeded by OCA on Tue Jul 29 16:15:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2mea.jpg|left|200px]]
+{{Seed}}
+[[Image:2mea.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2mea|  PDB=2mea  |  SCENE=  }}
-'''CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS'''
+===CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS===
-==Overview==
+<!--
-To elucidate correlative relationships between structural change and thermodynamic stability in proteins, a series of mutant human lysozymes modified at two buried positions (Ile56 and Ile59) were examined. Their thermodynamic parameters of denaturation and crystal structures were studied by calorimetry and X-ray crystallography. The mutants at positions 56 and 59 exhibited different responses to a series of amino acid substitutions. The changes in stability due to substitutions showed a linear correlation with changes in hydrophobicity of substituted residues, having different slopes at each mutation site. However, the stability of each mutant was found to be represented by a unique equation involving physical properties calculated from mutant structures. By fitting present and previous stability data for mutant human lysozymes substituted at various positions to the equation, the magnitudes of the hydrophobicity of a carbon atom and the hydrophobicity of nitrogen and neutral oxygen atoms were found to be 0.178 and -0.013 kJ/mol.A(2), respectively. It was also found that the contribution of a hydrogen bond with a length of 3.0 A to protein stability was 5.1 kJ/mol and the entropy loss of newly introduction of a water molecules was 7.8 kJ/mol.
+The line below this paragraph, {{ABSTRACT_PUBMED_10556244}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10556244 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10556244}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Hydrolase]]
 [[Category: O-glycosyl]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:32:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:15:54 2008''