1wqr

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[[Image:1wqr.gif|left|200px]]
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{{STRUCTURE_1wqr| PDB=1wqr | SCENE= }}
{{STRUCTURE_1wqr| PDB=1wqr | SCENE= }}
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'''CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME'''
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===CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME===
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==Overview==
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The contribution of hydrogen bonds to the conformational stability of human lysozyme was investigated by the combination of calorimetric and X-ray analyses of six Tyr --&gt; Phe mutants. Unfolding Delta G and unfolding Delta H values of the Tyr --&gt; Phe mutant proteins were changed by from +0.3 to -4.0 kJ/mol and from 0 to -16 kJ/mol, respectively, compared to those of the wild-type protein. The net contribution of a hydrogen bond at a specific site to stability (Delta Gwild/HB), considering factors affected by substitutions, was evaluated on the basis of X-ray structures of the mutant proteins. In the present study, one of six mutant proteins was suitable for evaluating the strength of the hydrogen bond. Delta Gwild/HB for the intramolecular hydrogen bond at Tyr124 was evaluated to be 7.5 kJ/mol. Results of the analysis of other mutants also suggest that hydrogen bonds of the hydroxyl group of Tyr, including the hydrogen bond with a water molecule, contribute to the stabilization of the human lysozyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 9649316 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9649316}}
==About this Structure==
==About this Structure==
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[[Category: Bacteriolytic enzyme]]
[[Category: Bacteriolytic enzyme]]
[[Category: Glycosidase]]
[[Category: Glycosidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:01:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:25:16 2008''

Revision as of 03:25, 28 July 2008

Image:1wqr.png

Template:STRUCTURE 1wqr

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

Template:ABSTRACT PUBMED 9649316

About this Structure

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

Reference

Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants., Yamagata Y, Kubota M, Sumikawa Y, Funahashi J, Takano K, Fujii S, Yutani K, Biochemistry. 1998 Jun 30;37(26):9355-62. PMID:9649316

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