A fast and simple method for calibrating the flip angle in hyperpolarized 13C MRS experiments
From The DNP-NMR Blog:
A fast and simple method for calibrating the flip angle in hyperpolarized 13C MRS experiments
Giovannetti, G., et al., A fast and simple method for calibrating the flip angle in hyperpolarized 13C MRS experiments. Concepts in Magnetic Resonance Part B: Magnetic Resonance Engineering, 2015: p. n/a-n/a.
http://dx.doi.org/10.1002/cmr.b.21282
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07-14-2015 02:59 AM
A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts
A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts
Mark V. Berjanskii and David S. Wishart
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja407509z/aop/images/medium/ja-2013-07509z_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja407509z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qRQjRZhXxAM
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09-23-2013 09:41 PM
[NMR paper] A simple method to measure protein side-chain mobility using NMR chemical shifts.
A simple method to measure protein side-chain mobility using NMR chemical shifts.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A simple method to measure protein side-chain mobility using NMR chemical shifts.
J Am Chem Soc. 2013 Sep 13;
Authors: Berjanskii MV, Wishart DS
Abstract
Protein side-chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein-protein,...
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09-17-2013 11:36 PM
[NMR paper] Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
J Biomol NMR. 2013 Mar 2;
Authors: Smet-Nocca C, Launay H, Wieruszeski JM, Lippens G, Landrieu I
Abstract
The Pin1 protein plays a critical role in the functional regulation of the hyperphosphorylated neuronal Tau protein in Alzheimer's disease and is by itself regulated by phosphorylation. We have...
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03-05-2013 03:25 PM
[NMR paper] A simple method using 31P-NMR spectroscopy for the study of protein phosphorylation.
A simple method using 31P-NMR spectroscopy for the study of protein phosphorylation.
Related Articles A simple method using 31P-NMR spectroscopy for the study of protein phosphorylation.
Brain Res Brain Res Protoc. 2000 Apr;5(2):182-9
Authors: Hirai H, Yoshioka K, Yamada K
Nonradioactive 31P-NMR spectroscopy has previously been used for the study of protein phosphorylations. However, the procedures does not seem to be easy for non-experts of this field, hence, this approach has not been widely used. We introduce here a simple protocol with...
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11-18-2010 09:15 PM
[NMR paper] The chemical shift index: a fast and simple method for the assignment of protein seco
The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.
Related Articles The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.
Biochemistry. 1992 Feb 18;31(6):1647-51
Authors: Wishart DS, Sykes BD, Richards FM
Previous studies by Wishart et al. have demonstrated that 1H NMR chemical shifts are strongly dependent on the character and nature of protein secondary structure. In particular, it has been...
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08-21-2010 11:41 PM
A simple method for measuring signs of 1HN chemical shift differences between ground
Abstract NMR relaxation dispersion spectroscopy is a powerful method for studying protein conformational dynamics whereby visible, ground and invisible, excited conformers interconvert on the millisecond time-scale. In addition to providing kinetics and thermodynamics parameters of the exchange process, the CPMG dispersion experiment also allows extraction of the absolute values of the chemical shift differences between interconverting states,
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A simple method using 31P-NMR spectroscopy for the study of protein phosphorylation - ScienceDirect.com
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