Related ArticlesEnsemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters.
Adv Exp Med Biol. 2015;870:123-147
Authors: Kragelj J, Blackledge M, Jensen MR
Abstract
Intrinsically disordered proteins (IDPs) perform their function despite their lack of well-defined tertiary structure. Residual structure has been observed in IDPs, commonly described as transient/dynamic or expressed in terms of fractional populations. In order to understand how the protein primary sequence dictates the dynamic and structural properties of IDPs and in general to understand how IDPs function, atomic-level descriptions are needed. Nuclear magnetic resonance spectroscopy provides information about local and long-range structure in IDPs at amino acid specific resolution and can be used in combination with ensemble descriptions to represent the dynamic nature of IDPs. In this chapter we describe sample-and-select approaches for ensemble modelling of local structural propensities in IDPs with specific emphasis on validation of these ensembles.
PMID: 26387101 [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
[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...
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09-07-2013 09:54 PM
[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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04-03-2013 08:22 PM
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>
</br>
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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Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters.
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