[NMR paper] Microsecond timescale protein dynamics: a combined solid-state NMR approach.
Microsecond timescale protein dynamics: a combined solid-state NMR approach.
Related Articles Microsecond timescale protein dynamics: a combined solid-state NMR approach.
Chemphyschem. 2017 Nov 17;:
Authors: Rovó P, Linser R
Abstract
Conformational exchange in proteins is a major determinant in protein functionality. In particular, the ?s-ms timescale is associated with enzymatic activity and interactions between biological molecules. We show here that a comprehensive data set of R1? relaxation dispersion profiles employing...
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11-19-2017 05:41 AM
[NMR paper] Synthesis of Isotopically Labelled All-Trans Retinals for DNP-Enhanced Solid State NMR Studies of Retinylidene Proteins.
Synthesis of Isotopically Labelled All-Trans Retinals for DNP-Enhanced Solid State NMR Studies of Retinylidene Proteins.
Related Articles Synthesis of Isotopically Labelled All-Trans Retinals for DNP-Enhanced Solid State NMR Studies of Retinylidene Proteins.
J Labelled Comp Radiopharm. 2017 Oct 28;:
Authors: Leeder AJ, Brown LJ, Becker-Baldus J, Mehler M, Glaubitz C, Brown RCD
Abstract
Three all-trans retinals containing multiple (13) C labels have been synthesised to enable DNP enhanced solid-state MAS NMR studies of novel...
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10-29-2017 02:06 PM
[NMR paper] Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Solid State Nucl Magn Reson. 2015 Sep 14;
Authors: Williams JK, Schmidt-Rohr K, Hong M
Abstract
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping (13)C chemical shift ranges between 100 and 160ppm,...
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10-07-2015 11:27 AM
[NMR paper] On the problem of resonance assignments in solid state NMR of uniformly (15)N,(13)C-labeled proteins.
On the problem of resonance assignments in solid state NMR of uniformly (15)N,(13)C-labeled proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif On the problem of resonance assignments in solid state NMR of uniformly (15)N,(13)C-labeled proteins.
J Magn Reson. 2015 Apr;253:166-72
Authors: Tycko R
Abstract
Determination of accurate resonance assignments from multidimensional chemical shift correlation spectra is one of the major problems in...
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03-24-2015 09:58 PM
On the problem of resonance assignments in solid state NMR of uniformly 15N,13C-labeled proteins
On the problem of resonance assignments in solid state NMR of uniformly 15N,13C-labeled proteins
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): Robert Tycko</br>
Determination of accurate resonance assignments from multidimensional chemical shift correlation spectra is one of the major problems in biomolecular solid state NMR, particularly for relative large proteins with less-than-ideal NMR linewidths. This article investigates the difficulty of resonance assignment, using a computational Monte Carlo/simulated...
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03-20-2015 01:48 AM
[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
An ensemble dynamics approach to decipher solid-state NMR observables of membrane proteins
An ensemble dynamics approach to decipher solid-state NMR observables of membrane proteins
February 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1818, Issue 2</br>
</br>
Solid-state NMR (SSNMR) is an invaluable tool for determining orientations of membrane proteins and peptides in lipid bilayers. Such orientational descriptions provide essential information about membrane protein functions. However, when a semi-static single conformer model is used to interpret various SSNMR observables, important dynamics information can...
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02-03-2013 10:13 AM
An ensemble dynamics approach to decipher solid-sate NMR observables of membrane proteins.
An ensemble dynamics approach to decipher solid-sate NMR observables of membrane proteins.
An ensemble dynamics approach to decipher solid-sate NMR observables of membrane proteins.
Biochim Biophys Acta. 2011 Aug 8;
Authors: Im W, Jo S, Kim T
Abstract
Solid-state NMR (SSNMR) is an invaluable tool for determining orientations of membrane proteins and peptides in lipid bilayers. Such orientational descriptions provide essential information about membrane protein functions. However, when a semi-static single conformer model is used to...
Dynamics of Uniformly Labelled Solid Proteins between 100-300 K: A 2D 2H-13C MAS NMR Approach
Linear Mode
