Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein

Proteins: Structure, Function and Genetics

Volumn 45, Issue 3, 2001, Pages 274-280

  Takano, Kazufumi ^a   Yamagata, Yuriko ^b   Yutani, Katsuhide ^a  

^a OSAKA UNIVERSITY   (Japan)

^b KUMAMOTO UNIVERSITY   (Japan)

Author keywords

Differential scanning calorimetry; Gibbs energy; Local constraints; Mutant protein; Ramachandran map; X ray crystallography

Indexed keywords

LYSOZYME; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; CALORIMETRY, DIFFERENTIAL SCANNING; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; HUMANS; MURAMIDASE; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 0035889693     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1147     Document Type: Article

References (26)

1. Stereochemistry of polypeptide chain configurations
2. Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units
3. Experimental observed conformation-dependent geometry and hidden strain in proteins
4. Occurrences of left-handed a-helical conformations in protein structures
5. Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme
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
7. Isolation and characterization of human milk lysozyme
8. A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
9. Contribution of hydrogen bonds to the conformational stability of human lysozyme: Calorimetry and X-ray analysis of six tyrosine→phenylalanine mutants
10. Contribution of water molecules in the interior of a protein to the conformational stability
11. 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
12. Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes
13. Contribution of salt bridges near the surface of a protein to the conformational stability
14. Contribution of polar groups in the interior of a protein to the conformational stability
15. Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions
16. Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme
17. Contribution of hydrogen bonds to the conformational stability of human lysozyme: Calorimetry and X-ray analysis of six Ser → Ala mutants
18. Role of amino acid residues at turns in the conformational stability and folding of human lysozyme
19. Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine
20. Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability
21. Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme
22. Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme
23. 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
24. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding