Native protein sequences are designed to destabilize folding intermediates

Biochemistry

Volumn 45, Issue 8, 2006, Pages 2488-2492

  Isogai, Yasuhiro ^a,b,c  

^a RIKEN HARIMA INSTITUTE   (Japan)

^b Japan Science and Technology Agency   (Japan)

^c RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; GENETIC ENGINEERING; HYDROPHOBICITY; MUTAGENESIS; THERMODYNAMIC STABILITY;

FOLDING INTERMEDIATES; HYDROPHOBIC RESIDUES; PROTEIN SEQUENCES; PROTEIN STABILITY; TRANSIENT FORMATION;

PROTEINS;

APOMYOGLOBIN; GLOBULAR PROTEIN; ISOLEUCINE; LEUCINE; VALINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; GENE MUTATION; HYDROPHOBICITY; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS; WHALE;

AMINO ACID SEQUENCE; ANIMALS; DOSE-RESPONSE RELATIONSHIP, DRUG; GUANIDINE; HYDROPHOBICITY; MOLECULAR SEQUENCE DATA; MUTATION; MYOGLOBIN; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPERM WHALE; STRUCTURAL HOMOLOGY, PROTEIN; THERMODYNAMICS;

CETACEA; PHYSETER CATODON;

EID: 33644546698     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0523714     Document Type: Article

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