A procedure is presented for the substantial simplification of 2D constant-time 13Câ??1H heteronuclear single-quantum correlation (HSQC) spectra of 13C-enriched proteins. In this approach, a single pulse sequence simultaneously records eight sub-spectra wherein the phases of the NMR signals depend on spin topology. Signals from different chemical groups are then stratified into different sub-spectra through linear combination based on Hadamard encoding of 13CHn multiplicity (nâ??=â??1, 2, and 3) and the chemical nature of neighboring 13C nuclei (aliphatic, carbonyl/carboxyl, aromatic). This results in five sets of 2D NMR spectra containing mutually exclusive signals from: (i) 13Cβâ??1Hβ correlations of asparagine and aspartic acid, 13Cγâ??1Hγ correlations of glutamine and glutamic acid, and 13Cαâ??1Hα correlations of glycine, (ii) 13Cαâ??1Hα correlations of all residues but glycine, and (iii) 13Cβâ??1Hβ correlations of phenylalanine, tyrosine, histidine, and tryptophan, and the remaining (iv) aliphatic 13CH2 and (v) aliphatic 13CH/13CH3 resonances. As HSQC is a common element of many NMR experiments, the spectral simplification proposed in this article can be straightforwardly implemented in experiments for resonance assignment and structure determination and should be of widespread utility.
Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements
Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements
Abstract
Magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy is a major technique for the characterization of the structural dynamics of biopolymers at atomic resolution. However, the intrinsic low sensitivity of this technique poses significant limitations to its routine application in structural biology. Here we achieve substantial savings in experimental time using a new subclass of...
[NMR paper] (2S,4R)- and (2S,4S)-perfluoro-tert-butyl 4-hydroxyproline: two conformationally distinct proline amino acids for sensitive application in 19F NMR.
(2S,4R)- and (2S,4S)-perfluoro-tert-butyl 4-hydroxyproline: two conformationally distinct proline amino acids for sensitive application in 19F NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles (2S,4R)- and (2S,4S)-perfluoro-tert-butyl 4-hydroxyproline: two conformationally distinct proline amino acids for sensitive application in 19F NMR.
J Org Chem. 2014 Jun 20;79(12):5880-6
Authors: Tressler CM, Zondlo NJ
Abstract
(2S,4R)- and...
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12-18-2014 11:22 PM
Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra
Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra
Abstract We have carried out chemical shift correlation experiments with symmetry-based mixing sequences at high MAS frequencies and examined different strategies to simultaneously acquire 3D correlation spectra that are commonly required in the structural studies of proteins. The potential of numerically optimised symmetry-based mixing sequences and the simultaneous recording of chemical shift correlation spectra such as: 3D NCAC and 3D NHH...
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11-29-2012 03:14 AM
A simplified recipe for assigning amide NMR signals using combinatorial (14)N amino acid inverse-labeling.
A simplified recipe for assigning amide NMR signals using combinatorial (14)N amino acid inverse-labeling.
A simplified recipe for assigning amide NMR signals using combinatorial (14)N amino acid inverse-labeling.
J Struct Funct Genomics. 2011 Aug 25;
Authors: Hiroaki H, Umetsu Y, Nabeshima YI, Hoshi M, Kohda D
Abstract
Assignment of backbone amide proton resonances is one of the most time-consuming stages of any protein NMR study when the protein samples behave non-ideally. A robust and convenient NMR procedure for analyzing spectra of...
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08-26-2011 04:22 PM
Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields
Sensitive 13Câ??13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields
Abstract Sensitive 2D solid-state 13Câ??13C correlation spectra of amyloid β fibrils have been recorded at very fast spinning frequencies and very high magnetic fields. It is demonstrated that PARIS-xy recoupling using moderate rf amplitudes can provide structural information by promoting efficient magnetization transfer even under such challenging experimental conditions. Furthermore, it has been shown both experimentally and by numerical simulations that the method is not...
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[NMR paper] Constant-time multidimensional electrophoretic NMR.
Constant-time multidimensional electrophoretic NMR.
Related Articles Constant-time multidimensional electrophoretic NMR.
J Magn Reson. 2002 Jun;156(2):181-6
Authors: Li E, He Q
Multidimensional electrophoretic NMR (ENMR) has been introduced to determine structures of coexisting proteins and protein conformations in solution. Signals of different proteins are separated in a new dimension of electrophoretic flow according to their characteristic electrophoretic mobilities. The electrophoretic interferograms have been generated in the flow...
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Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Exper
Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Experiment.
Related Articles Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Experiment.
Chem Phys Lett. 2010 Jul 9;494(1-3):104-110
Authors: Gopinath T, Veglia G
The atomic structure of small molecules and polypeptides can be attained from anisotropic NMR parameters such as dipolar couplings (DC) and chemical shifts (CS). Separated local field experiments resolve DC and CS correlations into two dimensions. However, crowded NMR...
Sensitive and simplified: a combinatorial acquisition of five distinct 2D constant-time 13 Câ?? 1 H NMR protein correlation spectra
Linear Mode
