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Angewandte Chemie - International Edition

Volumn 48, Issue 50, 2009, Pages 9452-9456

Unfolded-state structure and dynamics influence the fibril formation of human prion protein

(4) Gerum, Christian a Silvers, Robert a Wirmer Bartoschek, Julia a Schwalbe, Harald a

a GOETHE UNIVERSITY (Germany)

Author keywords

Conformational dynamics; Human prion protein; NMR spectroscopy; Protein structures

Indexed keywords

CONFORMATIONAL DYNAMICS; CYSTEINE RESIDUES; DISULFIDE BRIDGE; FIBRIL FORMATION; HOT SPOT; HUMAN PRION PROTEIN; NMR SPECTROSCOPY; NMR STUDIES; PROTEIN STRUCTURES; STRUCTURE AND DYNAMICS;

AMINO ACIDS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC ACIDS; SCANDIUM;

PROTEINS;

CYSTEINE; UREA;

ARTICLE; CHEMISTRY; HUMAN; KINETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PRION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION;

CYSTEINE; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION-REDUCTION; PRIONS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; UREA;

EID: 73249121817 PISSN: 14337851 EISSN: None Source Type: Journal
DOI: 10.1002/anie.200903771 Document Type: Article

Times cited : (26)

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