1ip5: Difference between revisions

Revision as of 13:44, 1 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:1ip5.png

Template:STRUCTURE 1ip5

G105A HUMAN LYSOZYMEG105A HUMAN LYSOZYME

Template:ABSTRACT PUBMED 11599030

About this StructureAbout this Structure

1IP5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein., Takano K, Yamagata Y, Yutani K, Proteins. 2001 Nov 15;45(3):274-80. PMID:11599030

Page seeded by OCA on Tue Jul 1 13:44:09 2008

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OCA

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-[[Image:1ip5.jpg|left|200px]]
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 {{STRUCTURE_1ip5|  PDB=1ip5  |  SCENE=  }}
-'''G105A HUMAN LYSOZYME'''
+===G105A HUMAN LYSOZYME===
-==Overview==
+<!--
-Our previous study of six non-Gly to Gly/Ala mutant human lysozymes in a left-handed helical region showed that only one non-Gly residue at a rigid site had unfavorable strain energy as compared with Gly at the same position (Takano et al., Proteins 2001; 44:233-243). To further examine the role of left-handed residues in the conformational stability of a protein, we constructed ten Gly to Ala mutant human lysozymes. Most Gly residues in human lysozyme are located in the left-handed helix region. The thermodynamic parameters for denaturation and crystal structures were determined by differential scanning calorimetry and X-ray analysis, respectively. The difference in denaturation Gibbs energy (DeltaDeltaG) for the ten Gly to Ala mutants ranged from + 1.9 to -7.5 kJ/mol, indicating that the effect of the mutation depends on the environment of the residue. We confirm that Gly in a left-handed region is more favorable at rigid sites than non-Gly, but there is little difference in energetic cost between Gly and non-Gly at flexible sites. The present results indicate that dihedral angles in the backbone conformation and also the flexibility at the position should be considered for analyses of protein stability, and protein structural determination, prediction, and design.
+The line below this paragraph, {{ABSTRACT_PUBMED_11599030}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11599030 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11599030}}
 ==About this Structure==
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 [[Category: Bacteriolytic enzyme]]
 [[Category: Glycosidase]]
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