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...
[NMR paper] Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues
NMR represents a key spectroscopic technique that contributes to the emerging field of highly flexible, intrinsically disordered proteins (IDPs) or protein regions (IDRs) that lack a stable three-dimensional structure. A set of exclusively heteronuclear NMR experiments tailored for proline residues, highly abundant in IDPs/IDRs, are presented here. They provide a valuable complement to the widely used approach based on amide proton detection, filling the gap...
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10-31-2023 10:49 AM
[NMR paper] Application of NMR to studies of intrinsically disordered proteins.
Application of NMR to studies of intrinsically disordered proteins.
Related Articles Application of NMR to studies of intrinsically disordered proteins.
Arch Biochem Biophys. 2017 May 11;:
Authors: Gibbs EB, Cook EC, Showalter SA
Abstract
The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins, and their clear functional advantages for signaling and gene regulation have created an imperative for high-resolution structural and mechanistic studies. NMR spectroscopy has played a central role...
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05-16-2017 10:27 PM
Application of NMR to studies of intrinsically disordered proteins
Application of NMR to studies of intrinsically disordered proteins
Publication date: Available online 11 May 2017
Source:Archives of Biochemistry and Biophysics</br>
Author(s): Eric B. Gibbs, Erik C. Cook, Scott A. Showalter</br>
The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins, and their clear functional advantages for signaling and gene regulation have created an imperative for high-resolution structural and mechanistic studies. NMR spectroscopy has played a central role in enhancing not only our understanding of...
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05-12-2017 05:13 PM
Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
From The DNP-NMR Blog:
Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
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Kurzbach, D., et al., Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water. Angew. Chem. Int. Ed., 2017. 56(1): p. 389-392.
http://dx.doi.org/10.1002/anie.201608903
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02-28-2017 12:02 AM
[NMR paper] Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
Investigation of Intrinsically Disordered Proteins through Exchange with Hyperpolarized Water
Hyperpolarized water can selectively enhance NMR signals of rapidly exchanging protons in osteopontin (OPN), a metastasis-associated intrinsically disordered protein (IDP), at near-physiological pH and temperature. The transfer of magnetization from hyperpolarized water is limited to solvent-exposed residues and therefore selectively enhances signals in 1H-15N correlation spectra. Binding to the polysaccharide heparin was found to induce the unfolding of preformed structural elements in OPN.A...
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12-05-2016 01:06 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
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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Optimal 13C NMR investigation of intrinsically disordered proteins at 1.2 GHz
Linear Mode
