dc.contributor.author | Allison, Jane R | |
dc.contributor.author | Hertig, Samuel | |
dc.contributor.author | Missimer, John H | |
dc.contributor.author | Smith, Lorna J | |
dc.contributor.author | Steinmetz, Michel O | |
dc.contributor.author | Dolenc, Jožica | |
dc.coverage.spatial | United States | |
dc.date.accessioned | 2022-05-24T22:29:38Z | |
dc.date.available | 2022-05-24T22:29:38Z | |
dc.date.issued | 2012-10 | |
dc.identifier.citation | (2012). Journal of Chemical Theory and Computation, 8(10), 3430-3444. | |
dc.identifier.issn | 1549-9618 | |
dc.identifier.uri | https://hdl.handle.net/2292/59490 | |
dc.description.abstract | NMR experiments provide detailed structural information about biological macromolecules in solution. However, the amount of information obtained is usually much less than the number of degrees of freedom of the macromolecule. Moreover, the relationships between experimental observables and structural information, such as interatomic distances or dihedral angle values, may be multiple-valued and may rely on empirical parameters and approximations. The extraction of structural information from experimental data is further complicated by the time- and ensemble-averaged nature of NMR observables. Combining NMR data with molecular dynamics simulations can elucidate and alleviate some of these problems, as well as allow inconsistencies in the NMR data to be identified. Here, we use a number of examples from our work to highlight the power of molecular dynamics simulations in providing a structural interpretation of solution NMR data. | |
dc.format.medium | Print-Electronic | |
dc.language | eng | |
dc.publisher | American Chemical Society (ACS) | |
dc.relation.ispartofseries | Journal of chemical theory and computation | |
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 | Generic health relevance | |
dc.subject | Science & Technology | |
dc.subject | Physical Sciences | |
dc.subject | Chemistry, Physical | |
dc.subject | Physics, Atomic, Molecular & Chemical | |
dc.subject | Chemistry | |
dc.subject | Physics | |
dc.subject | FREE R-VALUE | |
dc.subject | STRUCTURE REFINEMENT | |
dc.subject | DISTANCE RESTRAINTS | |
dc.subject | BIOMOLECULAR SIMULATION | |
dc.subject | SEQUENCE IDENTITY | |
dc.subject | GROMOS SOFTWARE | |
dc.subject | LOCAL-ELEVATION | |
dc.subject | TIME | |
dc.subject | CONSISTENT | |
dc.subject | COUPLINGS | |
dc.subject | 0601 Biochemistry and Cell Biology | |
dc.subject | 0306 Physical Chemistry (incl. Structural) | |
dc.subject | 0299 Other Physical Sciences | |
dc.subject | 0307 Theoretical and Computational Chemistry | |
dc.subject | 0803 Computer Software | |
dc.title | Probing the Structure and Dynamics of Proteins by Combining Molecular Dynamics Simulations and Experimental NMR Data. | |
dc.type | Journal Article | |
dc.identifier.doi | 10.1021/ct300393b | |
pubs.issue | 10 | |
pubs.begin-page | 3430 | |
pubs.volume | 8 | |
dc.date.updated | 2022-04-28T03:27:12Z | |
dc.rights.holder | Copyright: The author | en |
dc.identifier.pmid | 26592994 (pubmed) | |
pubs.author-url | https://www.ncbi.nlm.nih.gov/pubmed/26592994 | |
pubs.end-page | 3444 | |
pubs.publication-status | Published | |
dc.rights.accessrights | http://purl.org/eprint/accessRights/RestrictedAccess | en |
pubs.subtype | Journal Article | |
pubs.elements-id | 739591 | |
pubs.org-id | Science | |
pubs.org-id | Biological Sciences | |
dc.identifier.eissn | 1549-9626 | |
pubs.record-created-at-source-date | 2022-04-28 | |
pubs.online-publication-date | 2012-07-30 |
Showing items related by title, author, creator and subject.