How determinant is N-terminal to C-terminal coupling for protein folding?-Reference-Cited by-同舟云学术

How determinant is N-terminal to C-terminal coupling for protein folding?

Published:2015 Issue:5 Volume:17 Page:3512-3524
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Krobath Heinrich¹²³^ORCID,Rey Antonio⁴⁵⁶⁷⁸,Faísca Patrícia F. N.¹²³

Affiliation:

1. Centro de Física da Matéria Condensada and Departamento de Física

2. Faculdade de Ciências da Universidade de Lisboa

3. Portugal

4. Departamento de Química Física I

5. Facultad de Ciencias Químicas

6. Universidad Complutense

7. Madrid

8. Spain

Abstract

The existence of native interactions between the protein termini is a major determinant of the free energy barrier in a two-state folding transition being therefore a critical modulator of protein folding cooperativity.

Funder

Fundação para a Ciência e a Tecnologia

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CP/C4CP05178E

Reference73 articles.

1. Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. Wright

2. Topology, Stability, Sequence, and Length: Defining the Determinants of Two-State Protein Folding Kinetics

3. Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction11Edited by P. E. Wright

4. Prediction of folding rates and transition-state placement from native-state geometry

5. Principles that Govern the Folding of Protein Chains

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