1xqq
From Proteopedia
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| - | [[Image:1xqq.gif|left|200px]] | + | [[Image:1xqq.gif|left|200px]] |
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| - | '''Simultaneous determination of protein structure and dynamics''' | + | {{Structure |
| + | |PDB= 1xqq |SIZE=350|CAPTION= <scene name='initialview01'>1xqq</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Simultaneous determination of protein structure and dynamics''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XQQ is a [ | + | 1XQQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQQ OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15650731 15650731] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:19 2008'' |
Revision as of 13:13, 20 March 2008
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Simultaneous determination of protein structure and dynamics
Overview
We 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.
About this Structure
1XQQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 15:13:19 2008
