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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Cold Shock Protein A from Corynebacterium pseudotuberculosis: Role of Electrostatic Forces in the Stability of the Secondary Structure

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Author(s):
Coronado, Monika A. ; Caruso, Icaro P. ; de Oliveira, Vinicius M. ; Contessoto, Vinicius G. ; Leite, Vitor B. P. ; Kawai, Liege A. ; Arni, Raghuvir K. ; Eberle, Raphael J.
Total Authors: 8
Document type: Journal article
Source: PROTEIN AND PEPTIDE LETTERS; v. 24, n. 4, p. 358-367, 2017.
Web of Science Citations: 6
Abstract

The conformational stability of the Cold shock protein A (CspA) from C. pseudotuberculosis (Cp), a nucleic acid binding protein in function of pH and salt concentration was examined by using differential scanning calorimetry and CD spectroscopy in combination with computational analysis to identify the specify amino acids undergoing change. Our approach identified a sodiumbinding site in CpCspA and at pH 8.0 a significant reduction in the beta-sheet content was observed which resulted in a decrease of the protein thermal stability. The computational analyses identified His30 and His65 as the amino acids with the largest charge shifts at different pHs. His30/His65 are part of the extensive hydrogen bonding network and along with the ion-binding site are essential for the conformational stability of CspA. (AU)

FAPESP's process: 14/06862-7 - Computational studies in protein folding and enzymes engineering involved in bioethanol production
Grantee:Vitor Barbanti Pereira Leite
Support type: Regular Research Grants
FAPESP's process: 16/08104-8 - Structural and functional aspects of two DNA binding proteins encoded by Corynebacterium pseudotuberculosis
Grantee:Raphael Josef Eberle
Support type: Scholarships in Brazil - Post-Doctorate