Validation of protein backbone structures calculated from NMR angular restraints using Rosetta
Validation of protein backbone structures calculated from NMR angular restraints using Rosetta
Abstract
Multidimensional solid-state NMR spectra of oriented membrane proteins can be used to infer the backbone torsion angles and hence the overall protein fold by measuring dipolar couplings and chemical shift anisotropies, which depend on the orientation of each peptide plane with respect to the external magnetic field. However, multiple peptide plane orientations can be consistent with a given set of angular restraints. This ambiguity is further...
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05-11-2019 07:56 PM
ProteinNMR Structures Refined with Rosetta Have HigherAccuracy Relative to Corresponding X-ray Crystal Structures
ProteinNMR Structures Refined with Rosetta Have HigherAccuracy Relative to Corresponding X-ray Crystal Structures
Binchen Mao, Roberto Tejero, David Baker and Gaetano T. Montelione
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja409845w/aop/images/medium/ja-2013-09845w_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja409845w
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/7Lshnyi2_Vs
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01-24-2014 10:47 AM
[NMR paper] Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
J Am Chem Soc. 2014 Jan 6;
Authors: Mao B, Tejero R, Baker D, Montelione GT
Abstract
We have found that refinement of protein NMR structures using Rosetta with experimental NMR restraints yields more accurate protein NMR structures than those that have been deposited in the PDB using standard refinement...
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01-08-2014 11:23 AM
[NMR paper] An overview of tools for the validation of protein NMR structures.
An overview of tools for the validation of protein NMR structures.
An overview of tools for the validation of protein NMR structures.
J Biomol NMR. 2013 Jul 23;
Authors: Vuister GW, Fogh RH, Hendrickx PM, Doreleijers JF, Gutmanas A
Abstract
Biomolecular structures at atomic resolution present a valuable resource for the understanding of biology. NMR spectroscopy accounts for 11*% of all structures in the PDB repository. In response to serious problems with the accuracy of some of the NMR-derived structures and in order to facilitate...
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07-24-2013 04:52 PM
Local protein backbone folds determined by calculated NMR chemical shifts.
Local protein backbone folds determined by calculated NMR chemical shifts.
Local protein backbone folds determined by calculated NMR chemical shifts.
J Comput Chem. 2011 Sep 9;
Authors: Czajlik A, Hudáky I, Perczel A
Abstract
NMR chemical shifts (CSs: ?N(NH) , ?C(?) , ?C(?) , ?C', ?H(NH) , and ?H(?) ) were computed for the amino acid backbone conformers (?(L) , ?(L) , ?(L) , ?(L) , ?(L) , ?(D) , ?(D) , ?(D) , and ?(D) ) modeled by oligoalanine structures. Topological differences of the extended fold were investigated on single ?-strands,...