Minimization of cavity size ensures protein stability and folding: Structures of Phe46-replaced bovine pancreatic RNase A

Biochemistry

Volumn 42, Issue 36, 2003, Pages 10651-10658

  Kadonosono, Tetsuya ^a   Chatani, Eri ^a   Hayashi, Rikimaru ^a   Moriyama, Hideaki ^b   Ueki, Tatzuo ^c  

^a KYOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^c JAPAN SYNCHROTRON RADIATION RESEARCH INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS; HYDROPHOBICITY; THERMODYNAMIC STABILITY; X RAY CRYSTALLOGRAPHY;

FOLDING REACTION;

PROTEINS;

PANCREATIC RIBONUCLEASE; RIBONUCLEASE A;

AMINO ACID SEQUENCE; ARTICLE; CATTLE; ENZYME ACTIVE SITE; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CATTLE; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENZYME STABILITY; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; RIBONUCLEASE, PANCREATIC; THERMODYNAMICS;

BOS TAURUS; BOVINAE;

EID: 0041817974     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034499w     Document Type: Article

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