Abstract
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 intra peptide 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 intra peptide potentials and peptide-water potentials, and estimate the electrostatic solvation free energy of the system.
| Original language | English (US) |
|---|---|
| Article number | 23802 |
| Journal | Condensed Matter Physics |
| Volume | 19 |
| Issue number | 2 |
| DOIs | |
| State | Published - 2016 |
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Keywords
- Hydration free energy
- Oligoglycine collapse
ASJC Scopus subject areas
- Physics and Astronomy (miscellaneous)
- Condensed Matter Physics
Cite this
The contribution of electrostatic interactions to the collapse of oligoglycine in water. / Karandur, D.; Pettitt, Bernard.
In: Condensed Matter Physics, Vol. 19, No. 2, 23802, 2016.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The contribution of electrostatic interactions to the collapse of oligoglycine in water
AU - Karandur, D.
AU - Pettitt, Bernard
PY - 2016
Y1 - 2016
N2 - 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 intra peptide 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 intra peptide potentials and peptide-water potentials, and estimate the electrostatic solvation free energy of the system.
AB - 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 intra peptide 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 intra peptide potentials and peptide-water potentials, and estimate the electrostatic solvation free energy of the system.
KW - Hydration free energy
KW - Oligoglycine collapse
UR - http://www.scopus.com/inward/record.url?scp=84960910254&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84960910254&partnerID=8YFLogxK
U2 - 10.5488/CMP.19.23802
DO - 10.5488/CMP.19.23802
M3 - Article
AN - SCOPUS:84960910254
VL - 19
JO - Condensed Matter Physics
JF - Condensed Matter Physics
SN - 1607-324X
IS - 2
M1 - 23802
ER -