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

The folding process of the N-terminal domain of ribosomal protein L9 (NTL9) was investigated at constant-pH computer simulations. Evaluation of the role of electrostatic interaction during folding was carried out by including a Debye–Hückel potential into a C α structure-based model (SBM). In this...

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Veröffentlicht in:	Journal of chemical theory and computation 2016-07, Vol.12 (7), p.3270-3277
Hauptverfasser:	Contessoto, Vinícius G, de Oliveira, Vinícius M, de Carvalho, Sidney J, Oliveira, Leandro C, Leite, Vitor B. P
Format:	Artikel
Sprache:	eng
Schlagworte:	Computer simulation Constants Denaturation Electrostatics Folding Free energy Hydrogen-Ion Concentration Mathematical models Models, Molecular Protein Folding - drug effects Static Electricity
Online-Zugang:	Volltext
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