1xqq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Simultaneous determination of protein structure and dynamics== | ==Simultaneous determination of protein structure and dynamics== | ||
<StructureSection load='1xqq' size='340' side='right' caption='[[1xqq]], [[NMR_Ensembles_of_Models | 128 NMR models]]' scene=''> | <StructureSection load='1xqq' size='340' side='right'caption='[[1xqq]], [[NMR_Ensembles_of_Models | 128 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xqq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XQQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1xqq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XQQ FirstGlance]. <br> | ||
| Line 7: | Line 7: | ||
<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=1xqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqq OCA], [http://pdbe.org/1xqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xqq RCSB], [http://www.ebi.ac.uk/pdbsum/1xqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xqq ProSAT]</span></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=1xqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqq OCA], [http://pdbe.org/1xqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xqq RCSB], [http://www.ebi.ac.uk/pdbsum/1xqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xqq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 34: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Best, R B]] | [[Category: Best, R B]] | ||
[[Category: DePristo, M A]] | [[Category: DePristo, M A]] | ||
Revision as of 20:21, 22 January 2020
Simultaneous determination of protein structure and dynamicsSimultaneous determination of protein structure and dynamics
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe present a protocol for the experimental determination of ensembles of protein conformations that represent simultaneously the native structure and its associated dynamics. The procedure combines the strengths of nuclear magnetic resonance spectroscopy--for obtaining experimental information at the atomic level about the structural and dynamical features of proteins--with the ability of molecular dynamics simulations to explore a wide range of protein conformations. We illustrate the method for human ubiquitin in solution and find that there is considerable conformational heterogeneity throughout the protein structure. The interior atoms of the protein are tightly packed in each individual conformation that contributes to the ensemble but their overall behaviour can be described as having a significant degree of liquid-like character. The protocol is completely general and should lead to significant advances in our ability to understand and utilize the structures of native proteins. Simultaneous determination of protein structure and dynamics.,Lindorff-Larsen K, Best RB, Depristo MA, Dobson CM, Vendruscolo M Nature. 2005 Jan 13;433(7022):128-32. PMID:15650731[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||