Publication date: April 2014 Source:Journal of Magnetic Resonance, Volume 241
Author(s): Robert Konrat
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 of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This article will summarize key advances in basic physical-chemistry and NMR methodology, outline their limitations and envision future R&D directions. Graphical abstract
Toward optimal-resolution NMR of intrinsically disordered proteins
Toward optimal-resolution NMR of intrinsically disordered proteins
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Ji?í Nová?ek , Lukáš Žídek , Vladimír Sklená?</br>
Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15years. With the growing evidence of their important roles in fundamental cellular...
[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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[NMR paper] Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Structural characterization of intrinsically disordered proteins by NMR spectroscopy.
Molecules. 2013;18(9):10802-28
Authors: Kosol S, Contreras-Martos S, Cedeńo C, Tompa P
Abstract
Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and intrinsically disordered...
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[NMR paper] Describing intrinsically disordered proteins at atomic resolution by NMR.
Describing intrinsically disordered proteins at atomic resolution by NMR.
Related Articles Describing intrinsically disordered proteins at atomic resolution by NMR.
Curr Opin Struct Biol. 2013 Mar 29;
Authors: Jensen MR, Ruigrok RW, Blackledge M
Abstract
There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from...
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Describing intrinsically disordered proteins at atomic resolution by NMR
Describing intrinsically disordered proteins at atomic resolution by NMR
Available online 29 March 2013
Publication year: 2013
Source:Current Opinion in Structural Biology</br>
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There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the...
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03-29-2013 07:52 PM
Intrinsically disordered proteins - PhysicsToday.org
Intrinsically disordered proteins - PhysicsToday.org
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Intrinsically disordered proteins
PhysicsToday.org
Indeed, much of the community's understanding of protein function rests on our ability to deduce those structures by such methods as x-ray crystallography and nuclear magnetic resonance (NMR). The immense success and explanatory power of the ...
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08-01-2012 09:35 PM
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
J Biol Chem. 2011 Apr 20;
Authors: Iwasa H, Meshitsuka S, Hongo K, Mizobata T, Kawata Y
Co-chaperonin GroES from E. coli works with chaperonin GroEL to mediate the folding reactions of various proteins. However, under specific conditions, i. e., the...
NMR contributions to structural dynamics studies of intrinsically disordered proteins
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