[NMR paper] A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.
A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.
A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.
J Am Chem Soc. 2015 Sep 8;
Authors: Thiagarajan-Rosenkranz Paltr Uic Edu P, Draney AW, Smrt ST, Lorieau JL
Abstract
Residual Dipolar Couplings (RDCs) are integral to the refinement of membrane protein structures by NMR since they accurately define the orientation of helices and other structural...
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09-09-2015 11:49 AM
[NMR paper] Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.
Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.
Related Articles Solution NMR Experiment for Measurement of 15N-1H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.
J Am Chem Soc. 2015 Aug 21;
Authors: Eletsky A, Pulavarti SV, Beaumont V, Gollnick P, Szyperski T
Abstract
NMR residual dipolar couplings (RDCs) are exquisite probes of protein structure and dynamics. A new solution NMR experiment named 2D SE2 J-TROSY is presented to...
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08-22-2015 11:20 AM
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings
Abstract Residual dipolar couplings (RDCs) have the potential of providing detailed information about the conformational fluctuations of proteins. It is very challenging, however, to extract such information because of the complex relationship between RDCs and protein structures. A promising approach to decode this relationship involves structure-based calculations of the alignment tensors of protein conformations. By implementing this strategy to generate structural...
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06-26-2012 06:18 AM
Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins
Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins
Abstract A two-dimensional TROSY-based SIM-13Cmâ??1Hm/1Hâ??15N NMR experiment for simultaneous measurements of methyl 1 D CH and backbone amide 1 D NH residual dipolar couplings (RDC) in {U-; Ileδ1-; Leu,Val-}-labeled samples of large proteins is described. Significant variation in the alignment tensor of the 82-kDa enzyme Malate synthase G is observed as a function of only slight changes in experimental conditions. The SIM-13Cmâ??1Hm/1Hâ??15N data sets provide convenient means...
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09-30-2011 08:01 PM
Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins
Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins
Abstract It has been demonstrated that protein folds can be determined using appropriate computational protocols with NMR chemical shifts as the sole source of experimental restraints. While such approaches are very promising they still suffer from low convergence resulting in long computation times to achieve accurate results. Here we present a suite of time- and sensitivity optimized NMR experiments for rapid measurement of up to six RDCs per residue. Including such an RDC data set, measured in less...
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09-17-2011 10:20 AM
[NMR paper] Controlling residual dipolar couplings in high-resolution NMR of proteins by strain i
Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel.
Related Articles Controlling residual dipolar couplings in high-resolution NMR of proteins by strain induced alignment in a gel.
J Biomol NMR. 2001 Oct;21(2):141-51
Authors: Ishii Y, Markus MA, Tycko R
Water-soluble biological macromolecules can be weakly aligned by dissolution in a strained, hydrated gel such as cross-linked polyacrylamide, an effect termed 'strain-induced alignment in a gel' (SAG). SAG induces nonzero nuclear...
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11-19-2010 08:44 PM
[NMR paper] Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: d
Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin.
Related Articles Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin.
J Mol Biol. 2000 Feb 4;295(5):1265-73
Authors: Skrynnikov NR, Goto NK, Yang D, Choy WY, Tolman JR, Mueller GA, Kay LE
Protein function is often regulated...
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11-18-2010 09:15 PM
Theoretical framework for NMR residual dipolar couplings in unfolded proteins
Theoretical framework for NMR residual dipolar couplings in unfolded proteins
O. I. Obolensky, Kai Schlepckow, Harald Schwalbe and A. V. Solov’yov
Journal of Biomolecular NMR; 2007; 39(1) pp 1-16
Abstract:
A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arranged obstacles. For the case of bicelles oriented perpendicular to...
A PositivelyCharged Liquid Crystalline Medium forMeasuring Residual Dipolar Couplings in Membrane Proteins by NMR
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