Intrinsically disordered proteins (IDPs) are challenging established structural biology perception and urge a reassessment of the conventional understanding of the subtle interplay between protein structure and dynamics. Due to their importance in eukaryotic life and central role in protein interaction networks, IDP research is a fascinating and highly relevant research area in which NMR spectroscopy is destined to be a key player. The flexible nature of IDPs, as a result of the sampling of a vast conformational space, however, poses a tremendous scientific challenge, both technically and theoretically. Pronounced signal averaging results in narrow signal dispersion and requires higher dimensionality NMR techniques. Moreover, a fundamental problem in the structural characterization of IDPs is the definition of the conformational ensemble sampled by the polypeptide chain in solution, where often the interpretation relies on the concept of â??residual structureâ?? or â??conformational preferenceâ??. An important source of structural information is information-rich NMR experiments that probe protein backbone dihedral angles in a unique manner. Cross-correlated relaxation experiments have proven to fulfil this task as they provide unique information about protein backbones, particularly in IDPs. Here we present a novel cross-correlation experiment that utilizes non-uniform sampling detection schemes to resolve protein backbone dihedral ambiguities in IDPs. The sensitivity of this novel technique is illustrated with an application to the prototypical IDP \(\alpha\)-Synculein for which unexpected deviations from random-coil-like behaviour could be observed.
[NMR paper] A Novel High-Resolution and Sensitivity-Enhanced Three-Dimensional Solid-State NMR Experiment Under Ultrafast Magic Angle Spinning Conditions.
A Novel High-Resolution and Sensitivity-Enhanced Three-Dimensional Solid-State NMR Experiment Under Ultrafast Magic Angle Spinning Conditions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles A Novel High-Resolution and Sensitivity-Enhanced Three-Dimensional Solid-State NMR Experiment Under Ultrafast Magic Angle Spinning Conditions.
Sci Rep. 2015;5:11810
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[NMR paper] Three-dimensional structure of cyclic antibiotic teicoplanin aglycone using NMR distance and dihedral angle restraints in a DMSO solvation model.
Three-dimensional structure of cyclic antibiotic teicoplanin aglycone using NMR distance and dihedral angle restraints in a DMSO solvation model.
Three-dimensional structure of cyclic antibiotic teicoplanin aglycone using NMR distance and dihedral angle restraints in a DMSO solvation model.
Magn Reson Chem. 2015 Jul 1;
Authors: Gonnella NC, Grinberg N, Mcloughlin M, Choudhary O, Fandrick K, Ma S
Abstract
The three-dimensional solution conformation of teicoplanin aglycone was determined using NMR spectroscopy. A combination of...
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07-05-2015 02:07 AM
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
Abstract
Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY)...
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11-04-2014 01:02 AM
[NMR images] Table 1. Definition of dihedral angles, the expected dihedral angle ...
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Table 1. Definition of dihedral angles, the expected dihedral angle ...
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06-18-2013 07:21 AM
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
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02-21-2012 03:40 AM
[NMR paper] Resolving ambiguities in two-dimensional NMR spectra: the 'TILT' experiment.
Resolving ambiguities in two-dimensional NMR spectra: the 'TILT' experiment.
Related Articles Resolving ambiguities in two-dimensional NMR spectra: the 'TILT' experiment.
J Magn Reson. 2005 Feb;172(2):329-32
Authors: Kupce E, Freeman R
Ambiguities in two-dimensional nuclear magnetic resonance spectra due to overlap are usually resolved by recording a three-dimensional version of the experiment. It is shown that a simpler solution is to record a tilted projection of the three-dimensional spectrum, derived by Fourier transformation of the...
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11-24-2010 11:14 PM
[NMR paper] Automated NMR determination of protein backbone dihedral angles from cross-correlated
Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation.
Related Articles Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation.
J Biomol NMR. 2002 Apr;22(4):349-63
Authors: Kloiber K, Schüler W, Konrat R
The simultaneous interpretation of a suite of dipole-dipole and dipole-CSA cross-correlation rates involving the backbone nuclei 13Calpha, 1Halpha, 13CO, 15N and 1HN can be used to resolve the ambiguities associated with each individual...
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[NMR paper] HYPER: a hierarchical algorithm for automatic determination of protein dihedral-angle
HYPER: a hierarchical algorithm for automatic determination of protein dihedral-angle constraints and stereospecific C beta H2 resonance assignments from NMR data.
Related Articles HYPER: a hierarchical algorithm for automatic determination of protein dihedral-angle constraints and stereospecific C beta H2 resonance assignments from NMR data.
J Biomol NMR. 1999 Nov;15(3):251-64
Authors: Tejero R, Monleon D, Celda B, Powers R, Montelione GT
A new computer program, HYPER, has been developed for automated analysis of protein dihedral angle values...