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How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?
Mar 23, 2021 - 7:56 PM - by nmrlearner
nmrlearner's Avatar How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?

Abstract

The dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experimentsâ??where the sample is transferred to low fields for longitudinal (T1) relaxation, and back to high field for detection with residue-specific resolutionâ??seeks to increase the ability to distinguish the contributions from motion on timescales slower than a few nanoseconds. However, tumbling of a molecule in solution masks some of these motions. Therefore, we investigate to what extent relaxometry improves timescale resolution, using the â??detectorâ?? analysis of dynamics. Here, we demonstrate improvements in the characterization of internal dynamics of methyl-bearing side chains by carbon-13 relaxometry in the small protein ubiquitin. We show that relaxometry data leads to better information about nanosecond motions as compared to high-field relaxation data only. Our calculations show that gains from relaxometry are greater with increasing correlation time of rotational diffusion.



Source: Journal of Biomolecular NMR
0 Replies | 30 Views
[ASAP] Structure and Functionality of an Alkylated LixSiyOz Interphase for High-Energy Cathodes from DNP-ssNMR Spectroscopy
Mar 23, 2021 - 7:56 PM - by nmrlearner
nmrlearner's Avatar [ASAP] Structure and Functionality of an Alkylated LixSiyOz Interphase for High-Energy Cathodes from DNP-ssNMR Spectroscopy

Shira Haber, Rosy, Arka Saha, Olga Brontvein, Raanan Carmieli, Arava Zohar, Malachi Noked, and Michal Leskes



Journal of the American Chemical Society
DOI: 10.1021/jacs.1c00215



Source: Journal of the American Chemical Society
0 Replies | 25 Views
Atomic Techniques Reveal How Environment-Sensing Protein Allows Bacteria To Adapt - Technology Networks
Mar 23, 2021 - 7:56 PM - by nmrlearner
nmrlearner's Avatar Atomic Techniques Reveal How Environment-Sensing Protein Allows Bacteria To Adapt Technology Networks
Atomic Techniques Reveal How Environment-Sensing Protein Allows Bacteria To Adapt - Technology Networks
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0 Replies | 17 Views
Protein Crystallization & Crystallography Market Upcoming Challenges, Opportunities and Forecast, Global Size, Status and Forecast, Market Strategy, Outlook and Product Development, Market Segmentation By And Region, Type and Application - The Bi
Mar 23, 2021 - 7:56 PM - by nmrlearner
nmrlearner's Avatar Protein Crystallization & Crystallography Market Upcoming Challenges, Opportunities and Forecast, Global Size, Status and Forecast, Market Strategy, Outlook and Product Development, Market Segmentation By And Region, Type and Application - The Bisouv Network

Protein Crystallization & Crystallography Market Upcoming Challenges, Opportunities and Forecast, Global Size, Status and Forecast, Market Strategy, Outlook and Product Development, Market Segmentation By And Region, Type and Application The Bisouv Network Read here
0 Replies | 16 Views
[NMR paper] Magnetic graphene quantum dots facilitate closed-tube one-step detection of SARS-CoV-2 with ultra-low field NMR relaxometry
Mar 23, 2021 - 7:56 PM - by nmrlearner
nmrlearner's Avatar Magnetic graphene quantum dots facilitate closed-tube one-step detection of SARS-CoV-2 with ultra-low field NMR relaxometry

The rapid and sensitive diagnosis of the highly contagious severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is one of the crucial issues at the outbreak of the ongoing global pandemic that has no valid cure. Here, we propose a SARS-CoV-2 antibody conjugated magnetic graphene quantum dots (GQDs)-based magnetic relaxation switch (MRSw) that specifically recognizes the SARS-CoV-2. The probe of MRSw can be directly mixed with the test sample in a fully sealed vial without sample...

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0 Replies | 23 Views
[NMR paper] High-Resolution Studies of Proteins in Natural Membranes by Solid-State NMR
Mar 23, 2021 - 7:56 PM - by nmrlearner
nmrlearner's Avatar High-Resolution Studies of Proteins in Natural Membranes by Solid-State NMR

Membrane proteins are vital for cell function and thus represent important drug targets. Solid-state Nuclear Magnetic Resonance (ssNMR) spectroscopy offers a unique access to probe the structure and dynamics of such proteins in biological membranes of increasing complexity. Here, we present modern solid-state NMR spectroscopy as a tool to study structure and dynamics of proteins in natural lipid membranes and at atomic scale. Such spectroscopic studies profit from the use of high-sensitivity...

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0 Replies | 23 Views
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