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...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Institute for Condensed Matter Physics
2016-03-01
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| Series: | Condensed Matter Physics |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.5488/CMP.19.23802 |
| _version_ | 1818132877138722816 |
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| author | D. Karandur B.M. Pettitt |
| author_facet | D. Karandur B.M. Pettitt |
| author_sort | D. Karandur |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-11T08:43:48Z |
| format | Article |
| id | doaj.art-0de5d1735d9c4489a2d3ae6885f455a1 |
| institution | Directory Open Access Journal |
| issn | 1607-324X |
| language | English |
| last_indexed | 2024-12-11T08:43:48Z |
| publishDate | 2016-03-01 |
| publisher | Institute for Condensed Matter Physics |
| record_format | Article |
| series | Condensed Matter Physics |
| spelling | doaj.art-0de5d1735d9c4489a2d3ae6885f455a12022-12-22T01:14:11ZengInstitute for Condensed Matter PhysicsCondensed Matter Physics1607-324X2016-03-011922380210.5488/CMP.19.23802The contribution of electrostatic interactions to the collapse of oligoglycine in waterD. KarandurB.M. Pettitt 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.http://dx.doi.org/10.5488/CMP.19.23802hydration free energyoligoglycine collapse |
| spellingShingle | D. Karandur B.M. Pettitt The contribution of electrostatic interactions to the collapse of oligoglycine in water Condensed Matter Physics hydration free energy oligoglycine collapse |
| title | The contribution of electrostatic interactions to the collapse of oligoglycine in water |
| title_full | The contribution of electrostatic interactions to the collapse of oligoglycine in water |
| title_fullStr | The contribution of electrostatic interactions to the collapse of oligoglycine in water |
| title_full_unstemmed | The contribution of electrostatic interactions to the collapse of oligoglycine in water |
| title_short | The contribution of electrostatic interactions to the collapse of oligoglycine in water |
| title_sort | contribution of electrostatic interactions to the collapse of oligoglycine in water |
| topic | hydration free energy oligoglycine collapse |
| url | http://dx.doi.org/10.5488/CMP.19.23802 |
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