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1B5U

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT

Summary for 1B5U
Entry DOI10.2210/pdb1b5u/pdb
DescriptorPROTEIN (LYSOZYME), SODIUM ION (3 entities in total)
Functional Keywordshydrogen bond, stability, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P61626
Total number of polymer chains1
Total formula weight14727.68
Authors
Takano, K.,Yamagata, Y.,Kubota, M.,Funahashi, J.,Fujii, S.,Yutani, K. (deposition date: 1999-01-11, release date: 1999-01-20, Last modification date: 2024-10-09)
Primary citationTakano, K.,Yamagata, Y.,Kubota, M.,Funahashi, J.,Fujii, S.,Yutani, K.
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants.
Biochemistry, 38:6623-6629, 1999
Cited by
PubMed Abstract: 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.
PubMed: 10350481
DOI: 10.1021/bi9901228
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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數據於2024-11-06公開中

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