Folding of an all-helical Greek-key protein monitored by quenched-flow hydrogen-deuterium exchange and NMR spectroscopy

European Biophysics Journal

Volumn 41, Issue 1, 2012, Pages 41-51

  Greene, Lesley H ^a   Li, Hai ^a,b   Zhong, Junyan ^c   Zhao, Guoxia ^a   Wilson, Khym ^a  

^a OLD DOMINION UNIVERSITY   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

^c Old Dominion University   (United States)

Author keywords

Deuterium hydrogen exchange; Fas associated death domain; Greek key topology; NMR spectroscopy; Protein folding; Quenched flow

Indexed keywords

FAS ASSOCIATED DEATH DOMAIN PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DEUTERIUM HYDROGEN EXCHANGE; HUMAN; HYDROGEN BOND; KINETICS; NUCLEAR MAGNETIC RESONANCE; PH; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

DEUTERIUM EXCHANGE MEASUREMENT; FAS-ASSOCIATED DEATH DOMAIN PROTEIN; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84857361862     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-011-0756-6     Document Type: Article

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