13 C α CEST experiment on uniformly 13 C-labeled proteins
13 C α CEST experiment on uniformly 13 C-labeled proteins
Abstract
A new HSQC-based 13Cα CEST pulse scheme is proposed, which is suitable for uniformly 13C- or 13C, 15N-labeled samples in either water or heavy water. Except for Thr and Ser residues, the sensitivity of this scheme for uniformly labeled samples is similar to that of the previous scheme for selectively 13Cα-labeled samples with 100Â*% isotope enrichment. The experiment is demonstrated on an acyl carrier protein domain. Our 13Cα CEST data reveal that the minor state of the acyl...
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12-03-2014 04:05 PM
[NMR paper] Accurate measurements of (13)C-(13)C distances in uniformly (13)C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy.
Accurate measurements of (13)C-(13)C distances in uniformly (13)C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy.
Related Articles Accurate measurements of (13)C-(13)C distances in uniformly (13)C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy.
J Chem Phys. 2014 Sep 21;141(11):114201
Authors: Straasø LA, Nielsen JT, Bjerring M, Khaneja N, Nielsen NC
Abstract
Application of sets of (13)C-(13)C internuclear distance restraints...
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09-23-2014 01:57 PM
C4â?²/H4â?² selective, non-uniformly sampled 4D HC(P)CH experiment for sequential assignments of 13C-labeled RNAs
C4â?²/H4â?² selective, non-uniformly sampled 4D HC(P)CH experiment for sequential assignments of 13C-labeled RNAs
Abstract
A through bond, C4â?²/H4â?² selective, â??out and stayâ?? type 4D HC(P)CH experiment is introduced which provides sequential connectivity via H4â?²(i)â??C4â?²(i)â??C4â?²(iâ??1)â??H4â?²(iâ??1) correlations. The 31P dimension (used in the conventional 3D HCP experiment) is replaced with evolution of better dispersed C4â?² dimension. The experiment fully utilizes 13C-labeling of RNA by inclusion of two C4â?² evolution periods. An...
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09-11-2014 12:06 AM
[NMR paper] Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements.
Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements.
Related Articles Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements.
Protein Expr Purif. 2014 Mar 21;
Authors: Kroupa T, Prchal J, Doležal M, Ruml T, Hrabal R
Abstract
Nuclear magnetic resonance (NMR) is a powerful technique for solving protein structures orstudying their interactions. However, it requires molecules labeled with NMR sensitive isotopes like carbon(13)C and...
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03-26-2014 12:44 PM
Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements
Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements
Publication date: Available online 21 March 2014
Source:Protein Expression and Purification</br>
Author(s): Tomáš Kroupa , Jan Prchal , Michal Doležal , Tomáš Ruml , Richard Hrabal</br>
Nuclear magnetic resonance (NMR) is a powerful technique for solving protein structures orstudying their interactions. However, it requires molecules labeled with NMR sensitive isotopes like carbon13C and nitrogen15N. The recombinant expression of labeled proteins is simple...
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03-22-2014 01:28 AM
[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...
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06-21-2013 01:10 PM
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...
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03-10-2012 10:54 AM
An intraresidual i(HCA)CO(CA)NH experiment for the assignment of main-chain resonances in 15N, 13C labeled proteins
An intraresidual i(HCA)CO(CA)NH experiment for the assignment of main-chain resonances in 15N, 13C labeled proteins
Abstract An improved pulse sequence, intraresidual i(HCA)CO(CA)NH, is described for establishing solely 13Câ?²(i), 15N(i), 1HN(i) connectivities in uniformly 15N/13C-labeled proteins. In comparison to the â??out-and-backâ?? style intra-HN(CA)CO experiment, the new pulse sequence offers at least two-fold higher experimental resolution in the 13Câ?² dimension and on average 1.6 times higher sensitivity especially for residues in α-helices. Performance of the new experiment...
Erratum to: 13 C α CEST experiment on uniformly 13 C-labeled proteins
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