Related ArticlesRecombinant Intrinsically Disordered Proteins for NMR: Tips and Tricks.
Adv Exp Med Biol. 2015;870:187-213
Authors: Calçada EO, Korsak M, Kozyreva T
Abstract
The growing recognition of the several roles that intrinsically disordered proteins play in biology places an increasing importance on protein sample availability to allow the characterization of their structural and dynamic properties. The sample preparation is therefore the limiting step to allow any biophysical method being able to characterize the properties of an intrinsically disordered protein and to clarify the links between these properties and the associated biological functions.An increasing array of tools has been recruited to help prepare and characterize the structural and dynamic properties of disordered proteins. This chapter describes their sample preparation, covering the most common drawbacks/barriers usually found working in the laboratory bench. We want this chapter to be the bedside book of any scientist interested in preparing intrinsically disordered protein samples for further biophysical analysis.
PMID: 26387103 [PubMed - as supplied by publisher]
[NMR paper] An Approach to NMR Assignment of Intrinsically Disordered Proteins.
An Approach to NMR Assignment of Intrinsically Disordered Proteins.
An Approach to NMR Assignment of Intrinsically Disordered Proteins.
Chemphyschem. 2015 Jan 30;
Authors: Goradia N, Wiedemann C, Herbst C, Görlach M, Heinemann SH, Ohlenschläger O, Ramachandran R
Abstract
An efficient approach to NMR assignments in intrinsically disordered proteins is presented, making use of the good dispersion of cross peaks observed in - and -correlation spectra. The method involves the simultaneous collection of {3D (H)NCO(CAN)H and 3D...
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02-03-2015 12:16 PM
[NMR paper] In-cell (13)C NMR spectroscopy for the study of intrinsically disordered proteins.
In-cell (13)C NMR spectroscopy for the study of intrinsically disordered proteins.
In-cell (13)C NMR spectroscopy for the study of intrinsically disordered proteins.
Nat Protoc. 2014 Sep;9(9):2005-2016
Authors: Felli IC, Gonnelli L, Pierattelli R
Abstract
A large number of proteins carry out their function in highly flexible and disordered states, lacking a well-defined 3D structure. These proteins, referred to as intrinsically disordered proteins (IDPs), are now in the spotlight of modern structural biology. Nuclear magnetic...
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08-01-2014 06:21 PM
New 13C-detected experiments for the assignment of intrinsically disordered proteins
New 13C-detected experiments for the assignment of intrinsically disordered proteins
Abstract
NMR assignment of intrinsically disordered proteins (IDPs) by conventional HN-detected methods is hampered by the small dispersion of the amide protons chemical shifts and exchange broadening of amide proton signals. Therefore several alternative assignment strategies have been proposed in the last years. Attempting to seize that dispersion of 13Câ?˛ and 15N chemical shifts holds even in IDPs, we recently proposed two 13C-detected experiments to directly...
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06-19-2014 10:21 PM
[NMR paper] Toward optimal-resolution NMR of intrinsically disordered proteins.
Toward optimal-resolution NMR of intrinsically disordered proteins.
Related Articles Toward optimal-resolution NMR of intrinsically disordered proteins.
J Magn Reson. 2014 Apr;241:41-52
Authors: Nová?ek J, Zídek L, Sklená? V
Abstract
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...
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03-25-2014 11:49 AM
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...
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03-21-2014 12:52 AM
[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...
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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Recombinant Intrinsically Disordered Proteins for NMR: Tips and Tricks.
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