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Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1545, Issue 1-2, 2001, Pages 96-103

Differences in the pathways for unfolding and hydrogen exchange among mutants of Escherichia coli alkaline phosphatase

(5) Fischer, C J a,b Schauerte, J A a,c Wisser, K C a Steel, D G a,b Gafni, A a,c

a UNIVERSITY OF MICHIGAN HEALTH SYSTEM (United States)

b UNIVERSITY OF MICHIGAN (United States)

c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL (United States)

Author keywords

Hydrogen exchange; Phosphorescence; Protein folding

Indexed keywords

ALKALINE PHOSPHATASE; DEUTERIUM; GUANIDINE; HYDROGEN; MUTANT PROTEIN; TRYPTOPHAN;

AMINO ACID COMPOSITION; ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; TEMPERATURE DEPENDENCE;

ALKALINE PHOSPHATASE; BACTERIAL PROTEINS; DEUTERIUM; ESCHERICHIA COLI; GUANIDINE; HYDROGEN; HYDROGEN BONDING; KINETICS; LUMINESCENT MEASUREMENTS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; THERMODYNAMICS; TRYPTOPHAN;

ESCHERICHIA COLI;

EID: 0035830684 PISSN: 01674838 EISSN: None Source Type: Journal
DOI: 10.1016/S0167-4838(00)00266-1 Document Type: Article

Times cited : (2)

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