Cold Shock Protein A from Corynebacterium pseudotuberculosis: Role of Electrostatic Forces in the Stability of the Secondary Structure
| Autor: | Liege A. Kawai, Vinícius G. Contessoto, Raghuvir K. Arni, Raphael J. Eberle, Ícaro Putinhon Caruso, Vinícius M. de Oliveira, Vitor B. P. Leite, Monika A. Coronado |
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| Rok vydání: | 2017 |
| Předmět: |
Models
Molecular 0301 basic medicine Circular dichroism Static Electricity Biochemistry Protein Structure Secondary 03 medical and health sciences Ion binding Bacterial Proteins Structural Biology Thermal stability Protein secondary structure Histidine chemistry.chemical_classification Corynebacterium pseudotuberculosis Protein Stability Hydrogen bond Sodium General Medicine Hydrogen-Ion Concentration Cold-shock domain Recombinant Proteins Amino acid Crystallography 030104 developmental biology chemistry Biophysics Hydrogen Protein Binding |
| Zdroj: | Protein & Peptide Letters. 24:358-367 |
| ISSN: | 0929-8665 |
| Popis: | 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 β-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. |
| Databáze: | OpenAIRE |
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