A novel strategy for NMR resonance assignment and protein structure 
determination

Lemak, Alexander; Gutmanas, Aleksandras; Chitayat, Seth; Karra, Murthy; Farès, Christophe; Sunnerhagen, Maria; Arrowsmith, Cheryl H.

doi:10.1007/s10858-010-9458-0

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

このアイテムの新しいバージョンが利用可能です:
https://pure.mpg.de/pubman/item/item_1855282_2

詳細要約

公開

学術論文

A novel strategy for NMR resonance assignment and protein structure determination

MPS-Authors

/persons/resource/persons58537

Farès, Christophe
Ontario Cancer Institute and The Campbell Family Cancer Research Institute, Department of Medical Biophysics, University of Toronto;
The Northeast Structural Genomics Consortium, University of Toronto;
Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Lemak, A., Gutmanas, A., Chitayat, S., Karra, M., Farès, C., Sunnerhagen, M., & Arrowsmith, C. H. (2011). A novel strategy for NMR resonance assignment and protein structure determination. Journal of Biomolecular NMR, 49(1), 27-38. doi:10.1007/s10858-010-9458-0.

引用: https://hdl.handle.net/11858/00-001M-0000-0014-CA1B-8

要旨

The quality of protein structures determined by nuclear magnetic resonance (NMR) spectroscopy is contingent on the number and quality of experimentally-derived resonance assignments, distance and angular restraints. Two key features of protein NMR data have posed challenges for the routine and automated structure determination of small to medium sized proteins; (1) spectral resolution – especially of crowded nuclear Overhauser effect spectroscopy (NOESY) spectra, and (2) the reliance on a continuous network of weak scalar couplings as part of most common assignment protocols. In order to facilitate NMR structure determination, we developed a semi-automated strategy that utilizes non-uniform sampling (NUS) and multidimensional decomposition (MDD) for optimal data collection and processing of selected, high resolution multidimensional NMR experiments, combined it with an ABACUS protocol for sequential and side chain resonance assignments, and streamlined this procedure to execute structure and refinement calculations in CYANA and CNS, respectively. Two graphical user interfaces (GUIs) were developed to facilitate efficient analysis and compilation of the data and to guide automated structure determination. This integrated method was implemented and refined on over 30 high quality structures of proteins ranging from 5.5 to 16.5 kDa in size.