From the Cover: Consistent blind protein structure generation from NMR chemical shift data

@article{citeulike:2587380, abstract = {Protein NMR chemical shifts are highly sensitive to local structure. A robust protocol is described that exploits this relation for de novo protein structure generation, using as input experimental parameters the 13C{alpha}, 13C, 13C', 15N, 1H{alpha} and 1HN NMR chemical shifts. These shifts are generally available at the early stage of the traditional NMR structure determination process, before the collection and analysis of structural restraints. The chemical shift based structure determination protocol uses an empirically optimized procedure to select protein fragments from the Protein Data Bank, in conjunction with the standard ROSETTA Monte Carlo assembly and relaxation methods. Evaluation of 16 proteins, varying in size from 56 to 129 residues, yielded full-atom models that have 0.71.8 A root mean square deviations for the backbone atoms relative to the experimentally determined x-ray or NMR structures. The strategy also has been successfully applied in a blind manner to nine protein targets with molecular masses up to 15.4 kDa, whose conventional NMR structure determination was conducted in parallel by the Northeast Structural Genomics Consortium. This protocol potentially provides a new direction for high-throughput NMR structure determination. 10.1073/pnas.0800256105}, author = {Shen, Yang and Lange, Oliver and Delaglio, Frank and Rossi, Paolo and Aramini, James M. and Liu, Gaohua and Eletsky, Alexander and Wu, Yibing and Singarapu, Kiran K. and Lemak, Alexander and Ignatchenko, Alexandr and Arrowsmith, Cheryl H. and Szyperski, Thomas and Montelione, Gaetano T. and Baker, David and Bax, Ad }, citeulike-article-id = {2587380}, doi = {http://dx.doi.org/10.1073/pnas.0800256105}, journal = {Proceedings of the National Academy of Sciences}, keywords = {chemical, nmr, prediction, protein, shifts, structure}, month = {March}, number = {12}, pages = {4685--4690}, posted-at = {2008-07-05 20:30:20}, priority = {0}, title = {From the Cover: Consistent blind protein structure generation from NMR chemical shift data}, url = {http://dx.doi.org/10.1073/pnas.0800256105}, volume = {105}, year = {2008} }

TY - JOUR ID - citeulike:2587380 L3 - citeulike-article-id:2587380 N2 - Protein NMR chemical shifts are highly sensitive to local structure. A robust protocol is described that exploits this relation for de novo protein structure generation, using as input experimental parameters the 13C{alpha}, 13C, 13C', 15N, 1H{alpha} and 1HN NMR chemical shifts. These shifts are generally available at the early stage of the traditional NMR structure determination process, before the collection and analysis of structural restraints. The chemical shift based structure determination protocol uses an empirically optimized procedure to select protein fragments from the Protein Data Bank, in conjunction with the standard ROSETTA Monte Carlo assembly and relaxation methods. Evaluation of 16 proteins, varying in size from 56 to 129 residues, yielded full-atom models that have 0.71.8 A root mean square deviations for the backbone atoms relative to the experimentally determined x-ray or NMR structures. The strategy also has been successfully applied in a blind manner to nine protein targets with molecular masses up to 15.4 kDa, whose conventional NMR structure determination was conducted in parallel by the Northeast Structural Genomics Consortium. This protocol potentially provides a new direction for high-throughput NMR structure determination. 10.1073/pnas.0800256105 IS - 12 JF - Proceedings of the National Academy of Sciences EP - 4690 TI - From the Cover: Consistent blind protein structure generation from NMR chemical shift data VL - 105 SP - 4685 KW - chemical KW - nmr KW - prediction KW - protein KW - shifts KW - structure AU - Shen, Yang AU - Lange, Oliver AU - Delaglio, Frank AU - Rossi, Paolo AU - Aramini, James AU - Liu, Gaohua AU - Eletsky, Alexander AU - Wu, Yibing AU - Singarapu, Kiran AU - Lemak, Alexander AU - Ignatchenko, Alexandr AU - Arrowsmith, Cheryl AU - Szyperski, Thomas AU - Montelione, Gaetano AU - Baker, David AU - Bax, Ad PY - 2008/03/25/ UR - http://dx.doi.org/10.1073/pnas.0800256105 ER -