Authors: Nowakowski M, Saxena S, Stanek J, ?erko S, Ko?mi?ski W
Abstract
High dimensionality NMR experiments facilitate resonance assignment and precise determination of spectral parameters such as coupling constants. Sparse non-uniform sampling enables acquisition of experiments of high dimensionality with high resolution in acceptable time. In this review we present and compare some significant applications of NMR experiments of dimensionality higher than three in the field of biomolecular studies in solution.
Applications of high dimensionality experiments to biomolecular NMR
Applications of high dimensionality experiments to biomolecular NMR
Publication date: Available online 11 July 2015
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Micha? Nowakowski , Saurabh Saxena , Jan Stanek , Szymon ?erko , Wiktor Ko?mi?ski</br>
High dimensionality NMR experiments facilitate resonance assignment and precise determination of spectral parameters such as coupling constants. Sparse non-uniform sampling enables acquisition of experiments of high dimensionality with high resolution in acceptable time. In this review...
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07-12-2015 07:12 AM
[NMR paper] Reduced dimensionality (3,2)D NMR experiments and their automated analysis: implications to high-throughput structural studies on proteins.
Reduced dimensionality (3,2)D NMR experiments and their automated analysis: implications to high-throughput structural studies on proteins.
Related Articles Reduced dimensionality (3,2)D NMR experiments and their automated analysis: implications to high-throughput structural studies on proteins.
Magn Reson Chem. 2014 Sep 1;
Authors: Reddy JG, Kumar D, Hosur RV
Abstract
Protein NMR spectroscopy has expanded dramatically over the last decade into a powerful tool for the study of their structure, dynamics, and interactions. The...
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09-03-2014 11:44 AM
[NMR paper] High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
Related Articles High-dimensionality (13)C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.
J Biomol NMR. 2013 Nov 8;
Authors: Bermel W, Felli IC, Gonnelli L, Ko?mi?ski W, Piai A, Pierattelli R, Zawadzka-Kazimierczuk A
Abstract
We present three novel exclusively heteronuclear 5D (13)C direct-detected NMR experiments, namely (H(N-flip)N)CONCACON, (HCA)CONCACON and...
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11-11-2013 01:30 AM
[NMR paper] Reduced Dimensionality tailored HN(C)N Experiments for Facile Backbone Resonance Assignment of Proteins through Unambiguous Identification of Sequential HSQC Peaks
Reduced Dimensionality tailored HN(C)N Experiments for Facile Backbone Resonance Assignment of Proteins through Unambiguous Identification of Sequential HSQC Peaks
Publication date: Available online 8 October 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Dinesh Kumar</br>
Two novel reduced dimensionality (RD) tailored HN(C)N experiments are proposed to facilitate the backbone resonance assignment of proteins both in terms of its accuracy and speed. These experiments -referred here as (4,3)D-hNCOcaNH and (4,3)D-hNcoCANH- exploit the linear combination of...
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10-09-2013 05:31 AM
TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra
TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra
Abstract While NMR studies of proteins typically aim at structure, dynamics or interactions, resonance assignments represent in almost all cases the initial step of the analysis. With increasing complexity of the NMR spectra, for example due to decreasing extent of ordered structure, this task often becomes both difficult and time-consuming, and the recording of high-dimensional data with high-resolution may be essential. Random sampling of the evolution time space,...
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07-20-2012 11:13 PM
Aliasing in reduced dimensionality NMR spectra: (3,2)D HNHA and (4,2)D HN(COCA)NH experiments as examples
Aliasing in reduced dimensionality NMR spectra: (3,2)D HNHA and (4,2)D HN(COCA)NH experiments as examples
Abstract Reduced dimensionality NMR spectra usually require very large spectral widths in the shared dimension. In this paper we show that aliasing can be introduced in reduced dimensionality NMR spectra either to decrease the acquisition time or increase the resolution of the experiments without losing information. The gains of introducing aliasing are illustrated with two examples, the (3,2)D HNHA and the (4,2)D HN(COCA)NH experiments. In both cases a reduction of the spectral...
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01-09-2011 12:46 PM
[NMR paper] An emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
An emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
Related Articles An emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
Magn Reson Med Sci. 2002;1(1):27-31
Authors: Kuwata K
A new concept of protein dynamics has emerged quite recently, and a crucial link between protein dynamics and function has been largely established using recent NMR techniques in the solution state. Protein structure is governed by the thermodynamic principle and may not necessarily be unique in the...
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11-24-2010 08:49 PM
[NMR paper] Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignm
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Related Articles Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8009-14
Authors: Szyperski T, Yeh DC, Sukumaran DK, Moseley HN, Montelione GT
A suite of reduced-dimensionality (13)C,(15)N,(1)H-triple-resonance NMR experiments is presented for rapid and complete protein resonance assignment. Even when using short measurement times, these experiments allow one to retain...
Applications of high dimensionality experiments to biomolecular NMR.
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