The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems-Reference-Cited by-同舟云学术

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The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems

Published:2014 Issue:13 Volume:43 Page:4871-4893
ISSN:0306-0012
Container-title:Chem. Soc. Rev.
language:en
Short-container-title:Chem. Soc. Rev.

Author:

Sterpone Fabio¹²³⁴⁵,Melchionna Simone⁶⁷⁸⁹,Tuffery Pierre¹⁰³⁴¹¹,Pasquali Samuela¹²³⁴⁵,Mousseau Normand¹²¹³¹⁴,Cragnolini Tristan¹²³⁴⁵,Chebaro Yassmine¹²³⁴⁵,St-Pierre Jean-Francois¹²¹³¹⁴,Kalimeri Maria¹²³⁴⁵,Barducci Alessandro¹⁵¹⁶¹⁷,Laurin Yoann¹²³⁴⁵,Tek Alex¹²³⁴⁵,Baaden Marc¹²³⁴⁵,Nguyen Phuong Hoang¹²³⁴⁵,Derreumaux Philippe¹²³⁴⁵

Affiliation:

1. Laboratoire de Biochimie Théorique

2. UPR 9080 CNRS

3. Université Paris Diderot

4. Sorbonne Paris Cité

5. IBPC

6. Instituto Processi Chimico-Fisici

7. CNR-IPCF

8. Consiglio Nazionale delle Ricerche

9. Roma, Italy

10. INSERM U973

11. , France

12. Département de Physique

13. Université de Montréal

14. Montréal, Canada

15. Laboratoire de Physique Statistique

16. Ecole Polytechnique de Lausanne (EPFL)

17. CH-1015 Lausanne, Switzerland

Abstract

The OPEP coarse-grained protein model has been applied to a wide range of applications since its first release 15 years ago.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2014/CS/C4CS00048J

Reference317 articles.

1. Dynamics of folded proteins

2. Pathways to a Protein Folding Intermediate Observed in a 1-Microsecond Simulation in Aqueous Solution

3. How Fast-Folding Proteins Fold

4. Atomic-level description of ubiquitin folding

5. Structural basis for modulation of a G-protein-coupled receptor by allosteric drugs

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