1wqq

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spinqualitylabelsall models 1wqq, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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 --> Phe mutants. Unfolding Delta G and unfolding, Delta H values of the Tyr --> 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.

Disease

Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]

About this Structure

1WQQ is a Single protein structure of sequence from Homo sapiens with NA and CL as ligands. Active as Lysozyme, with EC number 3.2.1.17 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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