1b5y
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CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
OverviewOverview
To further examine the contribution of hydrogen bonds to the, conformational stability of the human lysozyme, six Ser to Ala mutants, were constructed. The thermodynamic parameters for denaturation of these, six Ser mutant proteins were investigated by differential scanning, calorimetry (DSC), and the crystal structures were determined by X-ray, analysis. The denaturation Gibbs energy (DeltaG) of the Ser mutant, proteins was changed from 2.0 to -5.7 kJ/mol, compared to that of the, wild-type protein. With an analysis in which some factors that affected, the stability due to mutation were considered, the contribution of, hydrogen bonds to the stability (Delta DeltaGHB) was extracted on the, basis of the structures of the mutant proteins. The results showed that, hydrogen bonds between protein atoms and between a protein atom and a, water bound with the protein molecule favorably contribute to the protein, stability. The net contribution of one intramolecular hydrogen bond to, protein stability (DeltaGHB) was 8.9 +/- 2.6 kJ/mol on average. However, the contribution to the protein stability of hydrogen bonds between a, protein atom and a bound water molecule was smaller than that for a bond, between protein atoms.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
1B5Y is a Single protein structure of sequence from Homo sapiens with NA as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants., Takano K, Yamagata Y, Kubota M, Funahashi J, Fujii S, Yutani K, Biochemistry. 1999 May 18;38(20):6623-9. PMID:10350481
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