[NMR paper] Optimal 13C NMR investigation of intrinsically disordered proteins at 1.2 GHz
Optimal 13C NMR investigation of intrinsically disordered proteins at 1.2 GHz
Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for characterizing biomolecules such as proteins and nucleic acids at atomic resolution. Increased magnetic field strengths drive progress in biomolecular NMR applications, leading to improved performance, e.g., higher resolution. A new class of NMR spectrometers with a 28.2 T magnetic field (1.2 GHz ąH frequency) has been commercially available since the end of 2019. The availability of ultra-high-field NMR instrumentation...
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12-14-2023 10:45 AM
[NMR paper] NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates
NMR insights into dynamic, multivalent interactions of intrinsically disordered regions: from discrete complexes to condensates
The spatial and temporal organization of interactions between proteins underlie the regulation of most cellular processes. The requirement for such interactions to be specific predisposes a view that protein-protein interactions are relatively static and are formed through the stable complementarity of the interacting partners. A growing body of reports indicate, however, that many interactions lead to fuzzy complexes with an ensemble of conformations in dynamic...
[NMR paper] Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy.
Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy.
Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy.
J Am Chem Soc. 2017 Dec 25;:
Authors: Delaforge E, Kragelj J, Tengo L, Palencia A, Milles S, Bouvignies G, Salvi N, Blackledge M, Jensen MR
Abstract
Intrinsically disordered proteins (IDPs) display a large number of interaction modes including folding-upon-binding, binding without major structural...
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12-26-2017 11:16 AM
[NMR paper] Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
Related Articles Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
J Am Chem Soc. 2016 Apr 26;
Authors: Abyzov A, Salvi N, Schneider R, Maurin D, Ruigrok RW, Jensen MR, Blackledge M
Abstract
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04-27-2016 01:51 PM
[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
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
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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