Contribution of Thr29 to the thermodynamic stability of goat α-lactalbumin as determined by experimental and theoretical approaches

Proteins: Structure, Function and Genetics

Volumn 45, Issue 1, 2001, Pages 16-29

  Horii, Katsunori ^a   Saito, Minoru ^b   Yoda, Takao ^c   Tsumoto, Kouhei ^a   Matsushima, Masaaki ^d   Kuwajima, Kunihiro ^c   Kumagai, Izumi ^a  

^a TOHOKU UNIVERSITY   (Japan)

^b HIROSAKI UNIVERSITY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d Rational Drug Design Laboratories   (Japan)

Author keywords

Free energy calculation; Molecular dynamics simulation; Protein stability; X ray crystallography

Indexed keywords

ALPHA LACTALBUMIN; MUTANT PROTEIN; RECOMBINANT PROTEIN; THREONINE;

AMINO ACID SUBSTITUTION; ARTICLE; CALCULATION; ENERGY; HYDROGEN BOND; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; SIMULATION; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; ANIMALS; CIRCULAR DICHROISM; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; GOATS; HYDROGEN BONDING; LACTALBUMIN; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; THREONINE;

CAPRA HIRCUS;

EID: 0035479434     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1119     Document Type: Article

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