| Title | A comparison of the different helices adopted by α- and β-peptides suggests different reasons for their stability |
| Publication Type | Journal Article |
| Year of Publication | 2010 |
| Authors | Allison, JR, Müller M, van Gunsteren WF |
| Volume | 19 |
| Pagination | 2186-2195 |
| Keywords | helix, molecular dynamics, peptide stability, α-peptide, β-peptide |
| Abstract | The right-handed α-helix is the dominant helical fold of α-peptides, whereas the left-handed 314-helix is the dominant helical fold of β-peptides. Using molecular dynamics simulations, the properties of α-helical α-peptides and 314-helical β-peptides with different C-terminal protonation states and in the solvents water and methanol are compared. The observed energetic and entropic differences can be traced to differences in the polarity of the solvent-accessible surface area and, in particular, the solute dipole moments, suggesting different reasons for their stability. |
| URL | http://dx.doi.org/10.1002/pro.504 |
A comparison of the different helices adopted by α- and β-peptides suggests different reasons for their stability
Publications by Jane Allison
2013.
Multiple binding modes for palmitate to barley lipid transfer protein facilitated by the presence of proline 12.
Protein Science.
22:
56-64
2013.
Directed Evolution of a Model Primordial Enzyme Provides Insights into the Development of the Genetic Code.
PLoS Genet.
9:
e1003187
2012.
Implicit solvation parameters derived from explicit water forces in large-scale Molecular Dynamics simulations.
J. Chem. Theory Comput..
:
2012.
Coarse-grained models for the solvents dimethyl sulfoxide, chloroform, and methanol.
The Journal of Chemical Physics.
136:
054505-11
2012.
Probing the structure and dynamics of proteins by combining molecular dynamics simulations and experimental NMR data.
J. Chem. Theory Comput..
:
2012.
Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.
Biophysical Reviews.
4:
189-203
