Nuclear magnetic resonance (NMR) spin relaxation experiments currently probe molecular motions on timescales from picoseconds to nanoseconds. The detailed interpretation of these motions in atomic detail benefits from complementarity with the results from molecular dynamics (MD) simulations. In this mini-review, we describe the recent developments in experimental techniques to study the backbone dynamics from ^(15)N relaxation and side-chain dynamics from ^(13)C relaxation, discuss the different...
[NMR paper] Recent progress of in-cell NMR of nucleic acids in living human cells.
Recent progress of in-cell NMR of nucleic acids in living human cells.
Related Articles Recent progress of in-cell NMR of nucleic acids in living human cells.
Biophys Rev. 2020 Mar 06;:
Authors: Yamaoki Y, Nagata T, Sakamoto T, Katahira M
Abstract
The inside of living cells is highly crowded with biological macromolecules. It has long been considered that the properties of nucleic acids and proteins, such as their structures, dynamics, interactions, and enzymatic activities, in intracellular environments are different from those...
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[NMR paper] Recent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria.
Recent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria.
Related Articles Recent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria.
Biochim Biophys Acta. 2017 Aug 24;:
Authors: Booth V, Warschawski DE, Santisteban NP, Laadhari M, Marcotte I
Abstract
Discoveries relating to innate immunity and antimicrobial peptides (AMPs) granted Bruce Beutler and Jules Hoffmann a Nobel prize in...
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[NMR paper] Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.
Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.
Related Articles Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.
J Biosci. 2016 Dec;41(4):787-803
Authors: Chiliveri SC, Deshmukh MV
Abstract
The advent of Transverse Relaxation Optimized SpectroscopY (TROSY) and perdeuteration allowed biomolecular NMR spectroscopists to overcome the size limitation barrier (approx. 20 kDa) in de novo structure determination of proteins. The utility of these techniques...
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12-15-2016 06:49 PM
Intrinsically disordered proteins I like to move it, move it - Nature.com
Intrinsically disordered proteins I like to move it, move it - Nature.com
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Intrinsically disordered proteins I like to move it, move it
Nature.com
Milles et al. used NMR spectroscopy to show that the ProXxxPheGly-rich domain of Nup153 (Nup153FGPxFG) is highly disordered in solution, with very little secondary structure. Only minor changes in the NMR spectrum were observed when importin β was ...
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11-18-2015 02:58 AM
Protein Dynamics from NMR Spectroscopy and MD Simulation
Protein Dynamics from NMR Spectroscopy and MD Simulation
29 January 2013
Publication year: 2013
Source:Biophysical Journal, Volume 104, Issue 2, Supplement 1</br>
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02-03-2013 10:13 AM
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Top Curr Chem. 2011 Sep 7;
Authors: Ishima R
Abstract
Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...
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09-08-2011 06:50 PM
[NMR paper] Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent p
Investigation of ligand-receptor systems by high-resolution solid-state NMR: recent progress and perspectives.
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Arch Pharm (Weinheim). 2005 Jun;338(5-6):217-28
Authors: Luca S, Heise H, Lange A, Baldus M
Solid-state Nuclear Magnetic Resonance (NMR) provides a general method to study molecular structure and dynamics in a non-crystalline and insoluble environment. We discuss the latest methodological progress to...
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11-25-2010 08:21 PM
[NMR paper] Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-
Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
Related Articles Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.
J Biomol Struct Dyn. 1999 Aug;17(1):157-74
Authors: Orekhov VY, Korzhnev DM, Pervushin KV, Hoffmann E, Arseniev AS
This paper presents a procedure for detection of intermediate nanosecond internal dynamics in globular proteins. The procedure uses 1H-15N relaxation measurements at several spectrometer frequencies...
How does it really move? Recent progress in the investigation of protein nanosecond dynamics by NMR and simulation
Linear Mode
