Relative free enthalpies for point mutations in two proteins with highly similar sequences but different folds.

Show simple item record

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/RetrictedAccess 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


Files in this item

Find Full text

This item appears in the following Collection(s)

Show simple item record

Share

Search ResearchSpace


Browse

Statistics