1XQQ
Simultaneous determination of protein structure and dynamics
Summary for 1XQQ
| Entry DOI | 10.2210/pdb1xqq/pdb |
| Related | 1D3Z 1UBQ |
| Descriptor | ubiquitin (1 entity in total) |
| Functional Keywords | signaling protein, ubiquitin |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 8576.83 |
| Authors | Lindorff-Larsen, K.,Best, R.B.,DePristo, M.A.,Vendruscolo, M.,Dobson, C.M. (deposition date: 2004-10-13, release date: 2005-02-08, Last modification date: 2024-05-29) |
| Primary citation | Lindorff-Larsen, K.,Best, R.B.,Depristo, M.A.,Dobson, C.M.,Vendruscolo, M. Simultaneous determination of protein structure and dynamics Nature, 433:128-132, 2005 Cited by PubMed Abstract: 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. PubMed: 15650731DOI: 10.1038/nature03199 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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