The contribution of electrostatic interactions to the collapse of oligoglycine in water
Protein solubility and conformational stability are a result of a balance of interactions both within a protein and between protein and solvent. The electrostatic solvation free energy of oligoglycines, models for the peptide backbone, becomes more favorable with an increasing length, yet longer pep...
Saved in:
| Date: | 2016 |
|---|---|
| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Published: |
Інститут фізики конденсованих систем НАН України
2016
|
| Series: | Condensed Matter Physics |
| Online Access: | http://dspace.nbuv.gov.ua/handle/123456789/155807 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Journal Title: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Cite this: | The contribution of electrostatic interactions to the collapse of oligoglycine in water / D. Karandur, B.M. Pettitt // Condensed Matter Physics. — 2016. — Т. 19, № 2. — С. 23802: 1–10. — Бібліогр.: 53 назв. — англ. |
Institution
Digital Library of Periodicals of National Academy of Sciences of Ukraine| Summary: | Protein solubility and conformational stability are a result of a balance of interactions both within a protein and between protein and solvent. The electrostatic solvation free energy of oligoglycines, models for the peptide backbone, becomes more favorable with an increasing length, yet longer peptides collapse due to the formation of favorable intrapeptide interactions between CO dipoles, in some cases without hydrogen bonds. The strongly repulsive solvent cavity formation is balanced by van der Waals attractions and electrostatic contributions. In order to investigate the competition between solvent exclusion and charge interactions we simulate the collapse of a long oligoglycine comprised of 15 residues while scaling the charges on the peptide from zero to fully charged. We examine the effect this has on the conformational properties of the peptide. We also describe the approximate thermodynamic changes that occur during the scaling both in terms of intrapeptide potentials and peptide-water potentials, and estimate the electrostatic solvation free energy of the system. |
|---|