Both the cis-trans equilibrium and isomerization dynamics of a single proline amide modulate β2-microglobulin amyloid assembly

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

Volumn 110, Issue 50, 2013, Pages 20051-20056

  Torbeev, Vladimir Yu ^a   Hilvert, Donald ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Amyloidogenesis; Native chemical ligation; Polymorphism; Protein conformation

Indexed keywords

AMIDE; AMYLOID; BETA 2 MICROGLOBULIN; PROLINE DERIVATIVE;

ARTICLE; ATOM; CHEMICAL COMPOSITION; CIRCULAR DICHROISM; CIS TRANS ISOMERISM; DYNAMICS; FLUORINE NUCLEAR MAGNETIC RESONANCE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HUMAN; ISOMERIZATION; MASS SPECTROMETRY; NUCLEAR OVERHAUSER EFFECT; OLIGOMERIZATION; PEPTIDE SYNTHESIS; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DENATURATION; PROTEIN UNFOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SYNTHESIS; TRANSMISSION ELECTRON MICROSCOPY;

EID: 84890285330     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1310414110     Document Type: Article

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