Oligomeric states along the folding pathways of β2-microglobulin: Kinetics, thermodynamics, and structure

Journal of Molecular Biology

Volumn 425, Issue 15, 2013, Pages 2722-2736

  Rennella, E ^a,b,c,d   Cutuil, T ^a,b,c,d   Schanda, P ^a,b,c,d   Ayala, I ^a,b,c,d   Gabel, F ^a,b,c,d   Forge, V ^b,c,d,e   Corazza, A ^f   Esposito, G ^f   Brutscher, B ^a,b,c,d  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b UNIV GRENOBLE ALPES   (France)

^c DIF   (France)

^d CNRS   (France)

^e CEA GRENOBLE   (France)

^f UNIVERSITY OF UDINE   (Italy)

Author keywords

folding amyloid formation; NMR; oligomers; real time; SAXS protein

Indexed keywords

BETA 2 MICROGLOBULIN; OLIGOMER; PROLINE;

ARTICLE; HETERONUCLEAR MULTIPLE QUANTUM COHERENCE; NITROGEN NUCLEAR MAGNETIC RESONANCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

EID: 84879973682     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.04.028     Document Type: Article

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