Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism-Reference-Cited by-同舟云学术

Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism

Published:2015 Issue:101 Volume:5 Page:83074-83088
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Adrover Miquel¹²³⁴⁵,Sanchis Pilar¹²³⁴⁵,Vilanova Bartolomé¹²³⁴⁵,Pauwels Kris⁶⁷⁸⁹¹⁰,Martorell Gabriel¹¹³⁴⁵,Pérez Juan Jesús¹²¹³¹⁴¹⁵⁵

Affiliation:

1. Institut Universitari d'Investigació en Ciències de la Salut (IUNICS)

2. Departament de Química

3. Universitat de les Illes Balears (UIB)

4. Palma de Mallorca

5. Spain

6. Structural Biology Brussels

7. Vrije Universiteit Brussels (VUB)

8. 1050 Brussels

9. Belgium

10. Structural Biology Research Centre

11. Serveis Científico-Tècnics

12. Departament d'Enginyeria Química

13. Universitat Politecnica de Catalunya (UPC)

14. ETSEIB

15. Barcelona

Abstract

NMR has been used to elucidate the folding pathway of neuromedin C and to characterize the architecture of the NMC–SDS micelle complex. Its C-terminal region is more prone to acquire an α-helical fold than the N-terminus, and it also binds to micelles.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/RA/C5RA12753J

Reference86 articles.

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