[NMR paper] Experiments with Direct Detection of Multiple FIDs
Experiments with Direct Detection of Multiple FIDs
Publication date: Available online 30 April 2019
Source: Journal of Magnetic Resonance
Author(s): ?riks Kup?e, Kaustubh R. Mote, Perunthiruthy K. Madhu
Abstract
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[ASAP] Characterization of Interactions and Phospholipid Transfer between Substrate Binding Proteins of the OmpC-Mla System
Characterization of Interactions and Phospholipid Transfer between Substrate Binding Proteins of the OmpC-Mla System
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00897/20181008/images/medium/bi-2018-00897d_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00897
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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11-25-2018 06:02 AM
[NMR paper] Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of 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 Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
J Phys Chem B. 2014 Mar 14;
Authors: Calligari PA, Abergel D
Abstract
Fluctuations of NMR resonance frequency shifts and their relation with protein exchanging conformations are usually...
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03-19-2014 10:43 PM
Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy
Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy
Abstract Relaxation violated coherence transfer NMR spectroscopy (Tugarinov et al. in J Am Chem Soc 129:1743â??1750, 2007) is an established experimental tool for quantitative estimation of the amplitudes of side-chain motions in methyl-protonated, highly deuterated proteins. Relaxation violated coherence transfer experiments monitor the build-up of methyl proton multiple-quantum coherences that can be created in magnetically equivalent...
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[NMR paper] Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiple
Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study.
Biochemistry. 1996 Jan 9;35(1):340-7
Authors: Avdulov NA, Chochina SV, Daragan VA, Schroeder F, Mayo KH, Wood WG
Molecular mechanisms of ethanol interaction with proteins are not well-understood. In the present study, direct...