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Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 11, 2006, Pages 4095-4100

The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates

(3) Bollen, Yves J M a Kamphuis, Monique B b,c Van Mierlo, Carlo P M b

a VU UNIVERSITY AMSTERDAM (Netherlands)

b WAGENINGEN UNIVERSITY (Netherlands)

c UTRECHT UNIVERSITY (Netherlands)

Author keywords

Hydrogen deuterium exchange; Partially unfolded forms; Protein folding

Indexed keywords

APOFLAVODOXIN; APOPROTEIN; DEUTERIUM; FLAVODOXIN; HYDROGEN; UNCLASSIFIED DRUG;

ARTICLE; ENERGY TRANSFER; ION EXCHANGE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARTIALLY UNFOLDED FORM; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

APOPROTEINS; AZOTOBACTER VINELANDII; BIOPHYSICS; DEUTERIUM; FLAVODOXIN; HYDROGEN; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; THERMODYNAMICS;

EID: 33645217096 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.0509133103 Document Type: Article

Times cited : (61)

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