[NMR paper] Determination of accurate backbone chemical shift tensors in microcrystalline proteins by integrating MAS NMR and QM/MM.
Determination of accurate backbone chemical shift tensors in microcrystalline proteins by integrating MAS NMR and QM/MM.
Related Articles Determination of accurate backbone chemical shift tensors in microcrystalline proteins by integrating MAS NMR and QM/MM.
Phys Chem Chem Phys. 2018 Mar 26;:
Authors: Fritz M, Quinn CM, Wang M, Hou G, Lu X, Koharudin LMI, Struppe J, Case DA, Polenova T, Gronenborn AM
Abstract
Chemical shifts are highly sensitive probes of local conformation and overall structure. Both isotropic shifts and...
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03-27-2018 09:54 PM
Xplor-NIH for Molecular Structure Determination from NMR and Other Data Sources
Xplor-NIH for Molecular Structure Determination from NMR and Other Data Sources
Abstract
Xplor-NIH is a popular software package for biomolecular structure determination from nuclear magnetic resonance (NMR) and other data sources. Here, some of Xplor-NIH's most useful data-associated energy terms are reviewed, including newer alternative options for using residual dipolar coupling data in structure calculations. Further, we discuss new developments in the implementation of strict symmetry for the calculation of symmetric homo-oligomers, and in the representation of the system as an...
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08-02-2017 02:19 PM
[NMR paper] NMR structure determination of proteins and protein complexes larger than 20 kDa.
NMR structure determination of proteins and protein complexes larger than 20 kDa.
Related Articles NMR structure determination of proteins and protein complexes larger than 20 kDa.
Curr Opin Chem Biol. 1998 Oct;2(5):564-70
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional nuclear magnetic resonance methodology to obtain 1H, 15N and 13C resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long-range order, coupled with new methods of structure refinement and novel methods...
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11-17-2010 11:15 PM
[NMR paper] An approach to global fold determination using limited NMR data from larger proteins
An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types.
An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types.
J Biomol NMR. 1996 Oct;8(3):360-8
Authors: Smith BO, Ito Y, Raine A, Teichmann S, Ben-Tovim L, Nietlispach D, Broadhurst RW, Terada T, Kelly M, Oschkinat H, Shibata T, Yokoyama S, Laue ED
A combination of calculation and experiment is used to demonstrate that the global fold of...
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08-22-2010 02:20 PM
[NMR paper] 1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 k
1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa.
Int J Biol Macromol. 1994 Oct;16(5):227-35
Authors: Gettins PG
The three-dimensional solution structures of proteins larger than about 25 kDa cannot at present be determined by multi-dimensional nuclear magnetic resonance (NMR) methods. However,...
NMR Structure Determination for Larger Proteins Using Backbone-Only Data - Science
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