2LJ5

Description of the Structural fluctuations of proteins from structure-based calculations of Residual dipolar couplings

2LJ5 の概要

• エントリーDOI: 10.2210/pdb2lj5/pdb
• 関連するPDBエントリー: 2KOX
• NMR情報: BMRB: 17919
• 分子名称: Ubiquitin (1 entity in total)
• 機能のキーワード: signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Ubiquitin: Cytoplasm (By similarity). 60S ribosomal protein L40: Cytoplasm (By similarity): P62987
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8576.83

構造登録者

De Simone, A.,Montalvao, R.,Vendruscolo, M. (登録日: 2011-09-06, 公開日: 2012-07-18, 最終更新日: 2024-05-01)

主引用文献

Montalvao, R.W.,De Simone, A.,Vendruscolo, M.
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings.
J.Biomol.Nmr, 53:281-292, 2012

PubMed Abstract: 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.

PubMed: 22729708
DOI: 10.1007/s10858-012-9644-3

実験手法

SOLUTION NMR