The dynamics of spin system coupled by chemical exchange between two sites with different chemical shifts during periodic radiofrequency (RF) irradiation was here investigated. When the instantaneous ?-flip of effective frequency during the course of frequency sweep was applied, a significant increase of exchange-induced relaxation rate constants was observed for small tip angle of magnetization in the laboratory frame of reference. This increase of the rate constants corresponds to the side bands generated by the periodic irradiation during the RF pulses. The exchange - induced relaxation rate constants depend on the exchange conditions, the RF power and the irradiation period. The described phenomenon promises applications for studying protein dynamics and for generating exchange specific relaxation contrasts in MRI.
[NMR paper] Radiofrequency fields in MAS solid state NMR probes.
Radiofrequency fields in MAS solid state NMR probes.
Radiofrequency fields in MAS solid state NMR probes.
J Magn Reson. 2017 Sep 06;284:20-32
Authors: Tošner Z, Purea A, Struppe JO, Wegner S, Engelke F, Glaser SJ, Reif B
Abstract
We present a detailed analysis of the radiofrequency (RF) field over full volume of a rotor that is generated in a solenoid coil. On top of the usually considered static distribution of amplitudes along the coil axis we describe dynamic radial RF inhomogeneities induced by sample rotation. During...
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Capturing a Dynamic Chaperone–Substrate Interaction Using NMR-Informed Molecular Modeling
Capturing a Dynamic Chaperone–Substrate Interaction Using NMR-Informed Molecular Modeling
Loi?c Salmon, Logan S. Ahlstrom, Scott Horowitz, Alex Dickson, Charles L. Brooks and James C. A. Bardwell
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b02382/20160802/images/medium/ja-2016-02382u_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02382
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ihnI-EXnn5s
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[NMR paper] Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling.
Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling.
Capturing a dynamic chaperone-substrate interaction using NMR-informed molecular modeling.
J Am Chem Soc. 2016 Jul 14;
Authors: Salmon L, Ahlstrom LS, Horowitz S, Dickson A, Brooks CL, Bardwell JC
Abstract
Chaperones maintain a healthy proteome by preventing aggregation and by aiding in protein folding. Precisely how chaperones influence the conformational properties of their substrates, however, remains unclear. To achieve a detailed...
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[NMR paper] Formation of periodic ?-turns in ?/?-hybrid peptides: DFT and NMR experimental evidence.
Formation of periodic ?-turns in ?/?-hybrid peptides: DFT and NMR experimental evidence.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles Formation of periodic ?-turns in ?/?-hybrid peptides: DFT and NMR experimental evidence.
Chem Asian J. 2014 Feb;9(2):457-61
Authors: Chandrasekhar S, Rao KV, Seenaiah M, Naresh P, Devi AS, Jagadeesh B
Abstract
Hybrid peptidic oligomers comprising natural and unnatural amino acid...
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[NMR paper] Capturing Conformational States in Proteins Using Sparse Paramagnetic NMR Data.
Capturing Conformational States in Proteins Using Sparse Paramagnetic NMR Data.
Related Articles Capturing Conformational States in Proteins Using Sparse Paramagnetic NMR Data.
PLoS One. 2015;10(5):e0127053
Authors: Pilla KB, Leman JK, Otting G, Huber T
Abstract
Capturing conformational changes in proteins or protein-protein complexes is a challenge for both experimentalists and computational biologists. Solution nuclear magnetic resonance (NMR) is unique in that it permits structural studies of proteins under greatly varying...