dc.contributor.author |
Allison, Jane R |
|
dc.contributor.author |
Müller, Marlen |
|
dc.contributor.author |
van Gunsteren, Wilfred F |
|
dc.coverage.spatial |
United States |
|
dc.date.accessioned |
2022-05-06T02:14:14Z |
|
dc.date.available |
2022-05-06T02:14:14Z |
|
dc.date.issued |
2010-11 |
|
dc.identifier.citation |
(2010). Protein Science, 19(11), 2186-2195. |
|
dc.identifier.issn |
0961-8368 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59007 |
|
dc.description.abstract |
The right-handed α-helix is the dominant helical fold of α-peptides, whereas the left-handed 3(14)-helix is the dominant helical fold of β-peptides. Using molecular dynamics simulations, the properties of α-helical α-peptides and 3(14)-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. |
|
dc.format.medium |
Print |
|
dc.language |
eng |
|
dc.publisher |
Wiley |
|
dc.relation.ispartofseries |
Protein science : a publication of the Protein Society |
|
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.subject |
Water |
|
dc.subject |
Methanol |
|
dc.subject |
Peptides |
|
dc.subject |
Nuclear Magnetic Resonance, Biomolecular |
|
dc.subject |
Protein Structure, Secondary |
|
dc.subject |
Hydrogen Bonding |
|
dc.subject |
Thermodynamics |
|
dc.subject |
Protein Stability |
|
dc.subject |
Molecular Dynamics Simulation |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Biochemistry & Molecular Biology |
|
dc.subject |
alpha-peptide |
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dc.subject |
beta-peptide |
|
dc.subject |
helix |
|
dc.subject |
peptide stability |
|
dc.subject |
molecular dynamics |
|
dc.subject |
MOLECULAR-DYNAMICS SIMULATIONS |
|
dc.subject |
GROMOS FORCE-FIELD |
|
dc.subject |
PARAMETRIZATION |
|
dc.subject |
SOLVATION |
|
dc.subject |
ENTROPIES |
|
dc.subject |
LIQUIDS |
|
dc.subject |
53A6 |
|
dc.subject |
0306 Physical Chemistry (incl. Structural) |
|
dc.subject |
0601 Biochemistry and Cell Biology |
|
dc.subject |
0802 Computation Theory and Mathematics |
|
dc.subject |
0899 Other Information and Computing Sciences |
|
dc.title |
A comparison of the different helices adopted by α- and β-peptides suggests different reasons for their stability. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1002/pro.504 |
|
pubs.issue |
11 |
|
pubs.begin-page |
2186 |
|
pubs.volume |
19 |
|
dc.date.updated |
2022-04-28T03:30:28Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
20853427 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/20853427 |
|
pubs.end-page |
2195 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Comparative Study |
|
pubs.subtype |
Research Support, Non-U.S. Gov't |
|
pubs.subtype |
research-article |
|
pubs.subtype |
Journal Article |
|
pubs.elements-id |
739608 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
dc.identifier.eissn |
1469-896X |
|
pubs.record-created-at-source-date |
2022-04-28 |
|
pubs.online-publication-date |
2010-10-26 |
|