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Volumn 40, Issue 12, 2001, Pages 3561-3571

NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding

(5) Yao, J b Chung, J a Eliezer, D c Wright, P E a Dyson, H J a

a SCRIPPS RESEARCH INSTITUTE (United States)

b GENENCOR INTERNATIONAL INC (United States)

c WEILL CORNELL MEDICAL COLLEGE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIC CHARACTERIZATIONS;

BIOELECTRIC POTENTIALS; CONFORMATIONS; DISPERSIONS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PH;

PROTEINS;

APOMYOGLOBIN; PEPTIDE; POLYPEPTIDE;

ARTICLE; CONFORMATIONAL TRANSITION; DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; WHALE;

ACETIC ACID; AMIDES; AMINO ACID SEQUENCE; ANIMALS; APOPROTEINS; CARBON ISOTOPES; HYDROCHLORIC ACID; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MYOGLOBIN; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTONS; REPRODUCIBILITY OF RESULTS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS; WHALES;

CETACEA;

EID: 0035957221 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi002776i Document Type: Article

Times cited : (210)

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