dc.contributor.author |
Hansen, Niels |
|
dc.contributor.author |
Allison, Jane R |
|
dc.contributor.author |
Hodel, Florian H |
|
dc.contributor.author |
van Gunsteren, Wilfred F |
|
dc.coverage.spatial |
United States |
|
dc.date.accessioned |
2022-05-25T04:16:05Z |
|
dc.date.available |
2022-05-25T04:16:05Z |
|
dc.date.issued |
2013-07-11 |
|
dc.identifier.citation |
(2013). Biochemistry, 52(29), 4962-4970. |
|
dc.identifier.issn |
0006-2960 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59497 |
|
dc.description.abstract |
Enveloping distribution sampling was used to calculate free-enthalpy changes associated with single amino acid mutations for a pair of proteins, GA95 and GB95, that show 95% sequence identity yet fold into topologically different structures. Of the L → A, I → F, and L → Y mutations at positions 20, 30, and 45, respectively, of the 56-residue sequence, the first and the last contribute the most to the free-enthalpy difference between the native and non-native sequence-structure combinations, in agreement with the experimental findings for this protein pair. The individual free-enthalpy changes are almost sequence-independent in the four-strand/one-helix structure, the stable form of GB95, while in the three-helix bundle structure, the stable form of GA95, an interplay between residues 20 and 45 is observed. |
|
dc.format.medium |
Print-Electronic |
|
dc.language |
eng |
|
dc.publisher |
American Chemical Society (ACS) |
|
dc.relation.ispartofseries |
Biochemistry |
|
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 |
Amino Acids |
|
dc.subject |
Proteins |
|
dc.subject |
Protein Folding |
|
dc.subject |
Point Mutation |
|
dc.subject |
Thermodynamics |
|
dc.subject |
Biotechnology |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Biochemistry & Molecular Biology |
|
dc.subject |
FREE-ENERGY CALCULATIONS |
|
dc.subject |
MOLECULAR-DYNAMICS SIMULATIONS |
|
dc.subject |
MONTE-CARLO METHOD |
|
dc.subject |
HYDRATION FREE-ENERGIES |
|
dc.subject |
FORCE-FIELD |
|
dc.subject |
AMINO-ACIDS |
|
dc.subject |
GENERALIZED-ENSEMBLE |
|
dc.subject |
STRUCTURE PREDICTION |
|
dc.subject |
COMPUTER-SIMULATION |
|
dc.subject |
EXPANDED ENSEMBLE |
|
dc.subject |
0601 Biochemistry and Cell Biology |
|
dc.subject |
0304 Medicinal and Biomolecular Chemistry |
|
dc.subject |
1101 Medical Biochemistry and Metabolomics |
|
dc.title |
Relative free enthalpies for point mutations in two proteins with highly similar sequences but different folds. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1021/bi400272q |
|
pubs.issue |
29 |
|
pubs.begin-page |
4962 |
|
pubs.volume |
52 |
|
dc.date.updated |
2022-04-28T03:22:40Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
23802564 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/23802564 |
|
pubs.end-page |
4970 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
|
pubs.subtype |
Journal Article |
|
pubs.elements-id |
739586 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
dc.identifier.eissn |
1520-4995 |
|
pubs.record-created-at-source-date |
2022-04-28 |
|
pubs.online-publication-date |
2013-07-11 |
|