Related ArticlesNMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
Adv Exp Med Biol. 2015;870:149-185
Authors: Kurzbach D, Kontaxis G, Coudevylle N, Konrat R
Abstract
Intrinsically disordered proteins (IDPs) are characterized by substantial conformational flexibility and thus not amenable to conventional structural biology techniques. Given their inherent structural flexibility NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This chapter will summarize key advances in NMR methodology. Despite the availability of efficient (multi-dimensional) NMR experiments for signal assignment of IDPs it is discussed that NMR of larger and more complex IDPs demands spectral simplification strategies capitalizing on specific isotope-labeling strategies. Prototypical applications of isotope labeling-strategies are described. Since IDP-ligand association and dissociation processes frequently occur on time scales that are amenable to NMR spectroscopy we describe in detail the application of CPMG relaxation dispersion techniques to studies of IDP protein binding. Finally, we demonstrate that the complementary usage of NMR and EPR data provide a more comprehensive picture about the conformational states of IDPs and can be employed to analyze the conformational ensembles of IDPs.
PMID: 26387102 [PubMed - as supplied by publisher]
NMR Studies of Dynamic Biomolecular Conformational Ensembles
NMR Studies of Dynamic Biomolecular Conformational Ensembles
Publication date: Available online 28 November 2014
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Dennis A. Torchia</br>
Multidimensional heteronuclear NMR approaches can provide nearly complete sequential signal assignments of isotopically enriched biomolecules. The availability of assignments together with measurements of spin relaxation rates, residual spin interactions, J-couplings and chemical shifts provides information at atomic resolution about internal dynamics on...
[NMR paper] NMR contributions to structural dynamics studies of intrinsically disordered proteins.
NMR contributions to structural dynamics studies of intrinsically disordered proteins.
Related Articles NMR contributions to structural dynamics studies of intrinsically disordered proteins.
J Magn Reson. 2014 Apr;241:74-85
Authors: Konrat R
Abstract
Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic...
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NMR contributions to structural dynamics studies of intrinsically disordered proteins
NMR contributions to structural dynamics studies of intrinsically disordered proteins
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Robert Konrat</br>
Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development...
[NMR paper] NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Related Articles NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Angew Chem Int Ed Engl. 2013 Sep 20;
Authors: Gil S, Hošek T, Solyom Z, Kümmerle R, Brutscher B, Pierattelli R, Felli IC
Abstract
When approaching physiological conditions, solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment...
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10-12-2013 05:24 PM
[NMR paper] NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles NMR based solvent exchange experiments to understand the conformational preference of intrinsically disordered proteins using FG-nucleoporin peptide as a model.
Biopolymers. 2013 Sep 4;
Authors: Heisel KA, Krishnan VV
...
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[NMR paper] Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts.
Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts.
Related Articles Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts.
Chemphyschem. 2013 Jun 21;
Authors: Kragelj J, Ozenne V, Blackledge M, Jensen MR
Abstract
The realization that a protein can be fully functional even in the absence of a stable three-dimensional structure has motivated a large number of studies describing the conformational behaviour of these proteins at atomic resolution. Here, we review...
NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
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