Methionine and alanine substitutions show that the formation of wild- type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate- limiting step in folding

Biochemistry

Volumn 38, Issue 44, 1999, Pages 14451-14460

  Gassner, Nadine C ^a   Baase, Walter A ^a   Lindstrom, Joel D ^a   Lu, Jirong ^a,b   Dahlquist, Frederick W ^a   Matthews, Brian W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b ELI LILLY AND COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE T4; CARBOXY TERMINAL SEQUENCE; ENZYME CONFORMATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

ALANINE; AMINO ACID SUBSTITUTION; BACTERIOPHAGE T4; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; KINETICS; METHIONINE; MODELS, MOLECULAR; MURAMIDASE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 0033517740     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9915519     Document Type: Article

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