[NMR paper] A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
Chembiochem. 2013 Jun 19;
Authors: Vallurupalli P, Bouvignies G, Kay LE
Abstract
Read the label: The NMR CEST experiment can be used to reconstruct spectra of sparsely populated, transiently formed protein conformers so long as they exchange with a highly populated ground state with rates of 20-300 s(-1) . Here we establish that accurate (13) C chemical shifts of side-chain carbon nuclei can be obtained from uniformly (13) C-labeled samples, without interference from the coupled (13) C spin network.
PMID: 23784752 [PubMed - as supplied by publisher]
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N–15N and carbonyl 13C–13C dipolar recoupling data
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N–15N and carbonyl 13C–13C dipolar recoupling data
May 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 218</br>
</br>
Recent structural studies of uniformly 15N, 13C-labeled proteins by solid state nuclear magnetic resonance (NMR) rely principally on two sources of structural restraints: (i) restraints on backbone conformation from isotropic 15N and 13C chemical shifts, based on empirical correlations between chemical shifts and...
nmrlearner
Journal club
0
02-03-2013 10:13 AM
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Kan-Nian Hu, Wei Qiang, Guillermo A. Bermejo, Charles D. Schwieters, Robert Tycko</br>
Recent structural studies of uniformly 15N,13C-labeled proteins by solid state nuclear magnetic resonance (NMR) rely principally on two sources of structural restraints: (i) restraints on backbone conformation from isotropic 15N and 13C chemical...
nmrlearner
Journal club
0
03-10-2012 10:54 AM
Alkali Metals in Ethylenediamine: A Computational Study of the Optical Absorption Spectra and NMR Parameters of [M(en)3?+·M?-] Ion Pairs
Alkali Metals in Ethylenediamine: A Computational Study of the Optical Absorption Spectra and NMR Parameters of Ion Pairs
Eva Zurek
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1085244/aop/images/medium/ja-2010-085244_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1085244
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iq3xbI47u0Y
nmrlearner
Journal club
0
03-03-2011 02:06 AM
[NMR paper] Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Related Articles Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
J Am Chem Soc. 2005 Aug 31;127(34):11946-7
Authors: Wylie BJ, Franks WT, Graesser DT, Rienstra CM
In this Communication, we introduce a 3D magic-angle spinning recoupling experiment that correlates chemical shift...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.
High-resolution solid-state NMR studies on uniformly -labeled ubiquitin.
Related Articles High-resolution solid-state NMR studies on uniformly -labeled ubiquitin.
Chembiochem. 2005 Sep;6(9):1638-47
Authors: Seidel K, Etzkorn M, Heise H, Becker S, Baldus M
Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly -labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by
NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.
Related Articles NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.
Proc Natl Acad Sci U S A. 1998 Nov 24;95(24):14147-51
Authors: Pervushin K, Ono A, Fernández C, Szyperski T, Kainosho M, Wüthrich K
This paper describes the NMR observation of 15N---15N and 1H---15N scalar couplings across the hydrogen bonds in Watson-Crick base pairs...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
MQ-HNCO-TROSY for the measurement of scalar and residual dipolar couplings in larger
Abstract We describe a novel pulse sequence, MQ-HNCO-TROSY, for the measurement of scalar and residual dipolar couplings between amide proton and nitrogen in larger proteins. The experiment utilizes the whole 2TN polarization transfer delay for labeling of 15N chemical shift in a constant time manner, which efficiently doubles the attainable resolution in 15N dimension with respect to the conventional HNCO-TROSY experiment. In addition, the accordion principle is employed for measuring (J + D)NHs, and the multiplet components are selected with the generalized version of the TROSY scheme...
nmrlearner
Journal club
0
08-14-2010 04:19 AM
S3EPY: a Sparky extension for determination of small scalar couplings from spin-state
Abstract S3EPY is a Python extension to the program Sparky written to facilitate the assessment of coupling constants from in-phase/antiphase and spin-state-selective excitation (S3E) experiments. It enables the routine use of small scalar couplings by automating the coupling evaluation procedure. S3EPY provides an integrated graphical user interface to programs which outputs graphs and the table of determined couplings.
Content Type Journal Article
DOI 10.1007/s10858-009-9392-1
Authors
Petr Novák, Masaryk University National Centre for Biomolecular Research, Faculty of Science...
A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
Linear Mode
