NTL9 Folding at Constant pH: The Importance of Electrostatic Interaction and pH Dependence-Reference-Cited by-同舟云学术

NTL9 Folding at Constant pH: The Importance of Electrostatic Interaction and pH Dependence

Published:2016-07-01 Issue:7 Volume:12 Page:3270-3277
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Contessoto Vinícius G.¹,de Oliveira Vinícius M.¹,de Carvalho Sidney J.¹,Oliveira Leandro C.¹,Leite Vitor B. P.¹

Affiliation:

1. Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas, Universidade Estadual Paulista (UNESP), São José do Rio Preto, São Paulo 15054-000, Brazil

Funder

Conselho Nacional de Desenvolvimento Cient?fico e Tecnol?gico

Funda??o de Amparo ? Pesquisa do Estado de S?o Paulo

Coordena??o de Aperfei?oamento de Pessoal de N?vel Superior

Pr?-Reitoria de Pesquisa, Universidade Estadual Paulista

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jctc.6b00399

Reference68 articles.

1. Electrostatic interactions in the denatured state ensemble: Their effect upon protein folding and protein stability

2. Nonnative Electrostatic Interactions Can Modulate Protein Folding: Molecular Dynamics with a Grain of Salt

3. Kinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain

4. The role of charged residues mediating low affinity protein-protein recognition at the cell surface by CD2

5. Protein Sliding along DNA: Dynamics and Structural Characterization

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