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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.

Takano K, Yamagata Y, Kubota M, Funahashi J, Fujii S, Yutani K
Biochemistry 38 6623-9 (1999)
Related entries: 1b5u, 1b5v, 1b5w, 1b5x, 1b5y

Cited: 39 times
EuropePMC logo PMID: 10350481

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.

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Related citations provided by authors (6)

  1. A General Rule for the Relationship between Hydrophobic Effect and Conformational Stability of a Protein: Stability and Structure of a Series of Hydrophobic Mutants of Human Lysozyme. Takano K, Yamagata Y, Yutani K J. Mol. Biol. 280 749- (1998)
  2. 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 37 9355- (1998)
  3. Contribution of the Hydrophobic Effect to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analyses of the Nine Valine to Alanine Mutants. Takano K, Yamagata Y, Fujii S, Yutani K Biochemistry 36 688- (1997)
  4. Contribution of Water Molecules in the Interior of a Protein to the Conformational Stability. Takano K, Funahashi J, Yamagata Y, Fujii S, Yutani K J. Mol. Biol. 274 132- (1997)
  5. The Structure, Stability, and Folding Process of Amyloidogenic Mutant Human Lysozyme. Funahashi J, Takano K, Ogasahara K, Yamagata Y, Yutani K J. Biochem. 120 1216- (1996)
  6. Contribution of Hydrophobic Residues to the Stability of Human Lysozyme: Calorimetric Studies and X-Ray Structural Analysis of the Five Isoleucine to Valine Mutants. Takano K, Ogasahara K, Kaneda H, Yamagata Y, Fujii S, Kanaya E, Kikuchi M, Oobatake M, Yutani K J. Mol. Biol. 254 62- (1995)

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