Structure and Dynamics of a Partially Folded Protein Are Decoupled from Its Mechanism of Aggregation-Reference-Cited by-同舟云学术

Structure and Dynamics of a Partially Folded Protein Are Decoupled from Its Mechanism of Aggregation

Published:2008-09-04 Issue:39 Volume:130 Page:13040-13050
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Calloni Giulia¹,Lendel Christofer¹,Campioni Silvia¹,Giannini Silva¹,Gliozzi Alessandra¹,Relini Annalisa¹,Vendruscolo Michele¹,Dobson Christopher M.¹,Salvatella Xavier¹,Chiti Fabrizio¹

Affiliation:

1. Dipartimento di Scienze Biochimiche, Università di Firenze, Viale Morgagni 50, 50134 Firenze, Italy, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K., Dipartimento di Fisica, Università di Genova and Consorzio Nazionale Interuniversitario per le Scienze Fisiche della Materia (CNISM), via Dodecaneso 33, I-16146, Genova, Italy, and Consorzio interuniversitrio “Istituto Nazionale Biostrutture e Biosistemi” (INBB), Viale delle Medaglie d’Oro 305, 00136 Roma, Italy

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja8029224

Reference59 articles.

1. Protein misfolding, evolution and disease

2. Conformational constraints for amyloid fibrillation: the importance of being unfolded

3. Protein Misfolding, Functional Amyloid, and Human Disease

4. The Yin and Yang of protein folding

5. Prevention of amyloid‐like aggregation as a driving force of protein evolution

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