2lj5
From Proteopedia
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| - | + | ==Description of the Structural fluctuations of proteins from structure-based calculations of Residual dipolar couplings== | |
| - | + | <StructureSection load='2lj5' size='340' side='right' caption='[[2lj5]], [[NMR_Ensembles_of_Models | 301 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2lj5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LJ5 FirstGlance]. <br> | |
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kox|2kox]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBA52, UBCEP2, RPS27A, UBA80, UBCEP1, UBB, UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lj5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lj5 RCSB], [http://www.ebi.ac.uk/pdbsum/2lj5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Residual dipolar couplings (RDCs) have the potential of providing detailed information about the conformational fluctuations of proteins. It is very challenging, however, to extract such information because of the complex relationship between RDCs and protein structures. A promising approach to decode this relationship involves structure-based calculations of the alignment tensors of protein conformations. By implementing this strategy to generate structural restraints in molecular dynamics simulations we show that it is possible to extract effectively the information provided by RDCs about the conformational fluctuations in the native states of proteins. The approach that we present can be used in a wide range of alignment media, including Pf1, charged bicelles and gels. The accuracy of the method is demonstrated by the analysis of the Q factors for RDCs not used as restraints in the calculations, which are significantly lower than those corresponding to existing high-resolution structures and structural ensembles, hence showing that we capture effectively the contributions to RDCs from conformational fluctuations. | ||
| - | + | Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings.,Montalvao RW, De Simone A, Vendruscolo M J Biomol NMR. 2012 Jun 23. PMID:22729708<ref>PMID:22729708</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | < | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Montalvao, R | + | [[Category: Montalvao, R]] |
| - | [[Category: Simone, A De | + | [[Category: Simone, A De]] |
| - | [[Category: Vendruscolo, M | + | [[Category: Vendruscolo, M]] |
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 13:45, 17 December 2014
Description of the Structural fluctuations of proteins from structure-based calculations of Residual dipolar couplings
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