dc.contributor.author |
Allison, Jane R |
|
dc.contributor.author |
Varnai, Peter |
|
dc.contributor.author |
Dobson, Christopher M |
|
dc.contributor.author |
Vendruscolo, Michele |
|
dc.coverage.spatial |
United States |
|
dc.date.accessioned |
2022-05-24T04:47:46Z |
|
dc.date.available |
2022-05-24T04:47:46Z |
|
dc.date.issued |
2009-12 |
|
dc.identifier.citation |
(2009). Journal of the American Chemical Society, 131(51), 18314-18326. |
|
dc.identifier.issn |
0002-7863 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59484 |
|
dc.description.abstract |
Natively unfolded proteins present a challenge for structure determination because they populate highly heterogeneous ensembles of conformations. A useful source of structural information about these states is provided by paramagnetic relaxation enhancement measurements by nuclear magnetic resonance spectroscopy, from which long-range interatomic distances can be estimated. Here we describe a method for using such distances as restraints in molecular dynamics simulations to obtain a mapping of the free energy landscapes of natively unfolded proteins. We demonstrate the method in the case of alpha-synuclein and validate the results by a comparison with electron transfer measurements. Our findings indicate that our procedure provides an accurate estimate of the relative statistical weights of the different conformations populated by alpha-synuclein in its natively unfolded state. |
|
dc.format.medium |
Print |
|
dc.language |
eng |
|
dc.publisher |
American Chemical Society (ACS) |
|
dc.relation.ispartofseries |
Journal of the American Chemical 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 |
Spin Labels |
|
dc.subject |
Magnetic Resonance Spectroscopy |
|
dc.subject |
Methods |
|
dc.subject |
Protein Conformation |
|
dc.subject |
Protein Denaturation |
|
dc.subject |
Thermodynamics |
|
dc.subject |
alpha-Synuclein |
|
dc.subject |
Molecular Dynamics Simulation |
|
dc.subject |
Science & Technology |
|
dc.subject |
Physical Sciences |
|
dc.subject |
Chemistry, Multidisciplinary |
|
dc.subject |
Chemistry |
|
dc.subject |
PARAMAGNETIC RELAXATION ENHANCEMENT |
|
dc.subject |
RESIDUAL DIPOLAR COUPLINGS |
|
dc.subject |
LONG-RANGE INTERACTIONS |
|
dc.subject |
MOLECULAR-DYNAMICS |
|
dc.subject |
STRUCTURAL-CHARACTERIZATION |
|
dc.subject |
STAPHYLOCOCCAL NUCLEASE |
|
dc.subject |
PARKINSONS-DISEASE |
|
dc.subject |
UNFOLDED PROTEINS |
|
dc.subject |
DENATURED STATE |
|
dc.subject |
NMR STRUCTURES |
|
dc.subject |
0306 Physical Chemistry (incl. Structural) |
|
dc.subject |
0299 Other Physical Sciences |
|
dc.subject |
03 Chemical Sciences |
|
dc.title |
Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1021/ja904716h |
|
pubs.issue |
51 |
|
pubs.begin-page |
18314 |
|
pubs.volume |
131 |
|
dc.date.updated |
2022-04-28T03:43:07Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
20028147 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/20028147 |
|
pubs.end-page |
18326 |
|
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 |
739613 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
dc.identifier.eissn |
1520-5126 |
|
pubs.record-created-at-source-date |
2022-04-28 |
|
pubs.online-publication-date |
2009-12-02 |
|