Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites
-
Altmetric Citations
Pearce, Benjamin J G; Jabar, Shereen; Loh, Choy-Theng; Szabo, Monika; Graham, Bim; Otting, Gottfried
Description
Pseudocontact shifts (PCS) encode long-range information on 3D structures of protein backbones and side-chains. The level of structural detail that can be obtained increases with the number of different sites tagged with a paramagnetic metal ion to generate PCSs. Here we show that PCSs from two different sites can suffice to determine the structure of polypeptide chains and their location and orientation relative to the magnetic susceptibility tensor χ, provided that PCSs are available for 1H...[Show more]
dc.contributor.author | Pearce, Benjamin J G | |
---|---|---|
dc.contributor.author | Jabar, Shereen | |
dc.contributor.author | Loh, Choy-Theng | |
dc.contributor.author | Szabo, Monika | |
dc.contributor.author | Graham, Bim | |
dc.contributor.author | Otting, Gottfried | |
dc.date.accessioned | 2018-10-18T03:06:13Z | |
dc.date.available | 2018-10-18T03:06:13Z | |
dc.identifier.issn | 0925-2738 | |
dc.identifier.uri | http://hdl.handle.net/1885/148497 | |
dc.description.abstract | Pseudocontact shifts (PCS) encode long-range information on 3D structures of protein backbones and side-chains. The level of structural detail that can be obtained increases with the number of different sites tagged with a paramagnetic metal ion to generate PCSs. Here we show that PCSs from two different sites can suffice to determine the structure of polypeptide chains and their location and orientation relative to the magnetic susceptibility tensor χ, provided that PCSs are available for 1H as well as heteronuclear spins. In addition, PCSs from two different sites are shown to provide detailed structural information on the conformation of methyl group-bearing amino-acid side-chains. A previously published ensemble structure of ubiquitin is shown to explain the magnetic susceptibility and alignment tensors slightly better than structures that try to explain the experimental data by a single conformation, illustrating the potential of PCSs as a tool to investigate small conformational changes. | |
dc.description.sponsorship | Financial support by the Australian Research Council is gratefully acknowledged. | |
dc.format.mimetype | application/pdf | |
dc.publisher | Springer Verlag | |
dc.source | Journal of biomolecular NMR | |
dc.subject | human ubiquitin | |
dc.subject | lanthanide tag | |
dc.subject | pseudocontact shift | |
dc.subject | residual anisotropic chemical shifts | |
dc.subject | structure determination | |
dc.subject | amino acids, branched-chain | |
dc.subject | lanthanoid series elements | |
dc.subject | nuclear magnetic resonance, biomolecular | |
dc.subject | protein conformation | |
dc.subject | proteins | |
dc.subject | ubiquitin | |
dc.title | Structure restraints from heteronuclear pseudocontact shifts generated by lanthanide tags at two different sites | |
dc.type | Journal article | |
local.identifier.citationvolume | 68 | |
dc.date.issued | 2017-05 | |
local.identifier.ariespublication | a383154xPUB6977 | |
local.publisher.url | https://link.springer.com | |
local.type.status | Accepted Version | |
local.contributor.affiliation | Pearce, B. J. G., Research School of Chemistry, The Australian National University | |
local.contributor.affiliation | Jabar, S., Research School of Chemistry, The Australian National University | |
local.contributor.affiliation | Loh, C.-T., Research School of Chemistry, The Australian National University | |
local.contributor.affiliation | Otting, G., Research School of Chemistry, The Australian National University | |
local.identifier.essn | 1573-5001 | |
local.bibliographicCitation.issue | 1 | |
local.bibliographicCitation.startpage | 19 | |
local.bibliographicCitation.lastpage | 32 | |
local.identifier.doi | 10.1007/s10858-017-0111-z | |
dcterms.accessRights | Open Access | |
dc.provenance | © Springer Science+Business Media Dordrecht 2017. http://www.sherpa.ac.uk/romeo/issn/0925-2738/..."Author's post-print on any open access repository after 12 months after publication" from SHERPA/RoMEO site (as at 18/10/18). This is a post-peer-review, pre-copyedit version of an article published in Journal of biomolecular NMR. The final authenticated version is available online at: http://dx.doi.org/10.1007/s10858-017-0111-z | |
Collections | ANU Research Publications |
Download
File | Description | Size | Format | Image |
---|---|---|---|---|
JBiomolNMR2017_68_19.pdf | Author/s Accepted Manuscript (AAM) / Post-print | 7.84 MB | Adobe PDF |
Items in Open Research are protected by copyright, with all rights reserved, unless otherwise indicated.
Updated: 17 November 2022/ Responsible Officer: University Librarian/ Page Contact: Library Systems & Web Coordinator