Three-dimensional HNCO and HNCA subspectra from a small protein (agitoxin, 4 kDa, enriched in carbon-13 and nitrogen-15), have been obtained by direct frequency-domain excitation of selected carbon and nitrogen sites. This new technique applies an array of several simultaneous soft radiofrequency spin-inversion pulses, encoded (on or off) according to nested Hadamard matrices, and the resulting responses are extracted by reference to the same matrices. This not only simplifies the spectra but, by avoiding extensive sampling in the traditional evolution dimensions, affords a speed advantage of more than two orders of magnitude.
Multi-dimensional NMR without coherence transfer: Minimizing losses in large systems.
Multi-dimensional NMR without coherence transfer: Minimizing losses in large systems.
Multi-dimensional NMR without coherence transfer: Minimizing losses in large systems.
J Magn Reson. 2011 Jul 21;
Authors: Liu Y, Prestegard JH
Most multi-dimensional solution NMR experiments connect one dimension to another using coherence transfer steps that involve evolution under scalar couplings. While experiments of this type have been a boon to biomolecular NMR the need to work on ever larger systems pushes the limits of these procedures. Spin relaxation...
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08-13-2011 12:57 PM
Analysis of non-uniformly sampled spectra with Multi-Dimensional Decomposition
Analysis of non-uniformly sampled spectra with Multi-Dimensional Decomposition
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 24 February 2011</br>
Vladislav Yu., Orekhov , Victor A., Jaravine</br>
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02-26-2011 01:07 PM
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
Abstract NMR spectroscopy has distinct advantages for providing insight into protein structures, but faces significant resolution challenges as protein size increases. To alleviate such resonance overlap issues, the ability to produce segmentally labeled proteins is beneficial. Here we show that the S. aureus transpeptidase sortase A can be used to catalyze the ligation of two separately expressed domains of the same protein, MecA (B. subtilis). The yield of purified, segmentally...
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12-31-2010 08:38 PM
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy.
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy.
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy.
J Biomol NMR. 2010 Dec 29;
Authors: Refaei MA, Combs A, Kojetin DJ, Cavanagh J, Caperelli C, Rance M, Sapitro J, Tsang P
NMR spectroscopy has distinct advantages for providing insight into protein structures, but faces significant resolution challenges as protein size increases. To alleviate such resonance overlap issues, the ability to...
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12-29-2010 04:04 PM
[NMR paper] Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic eve
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
Related Articles Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
J Am Chem Soc. 2005 Jun 8;127(22):8014-5
Authors: Schanda P, Brutscher B
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle...
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11-25-2010 08:21 PM
Combining methods for speeding up multi-dimensional acquisition. Sparse sampling and
Combining methods for speeding up multi-dimensional acquisition. Sparse sampling and fast pulsing methods for unfolded proteins
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 12 June 2010</br>
Dominique, Marion</br>
Resonance assignment of intrinsically disordered proteins is made difficult by the extensive spectral overlaps. High-resolution 3D and 4D spectra are thus essential for this purpose. We have adapted the series of 3D BEST experiments proposed by Lescop et al to the case of unfolded proteins. Longer acquisitions...
Fast multi-dimensional NMR of proteins.
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