Related ArticlesSolution NMR views of dynamical ordering of biomacromolecules.
Biochim Biophys Acta. 2017 Aug 25;:
Authors: Ikeya T, Ban D, Lee D, Ito Y, Kato K, Griesinger C
Abstract
BACKGROUND: To understand the mechanisms related to the 'dynamical ordering' of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can investigate biophysical events at the atomic level, in near-physiological buffer solutions, or even inside cells. Scope of Review In the past several decades, progress in solution NMR has significantly contributed to the elucidation of three-dimensional structures, the understanding of conformational motions, and the underlying thermodynamic and kinetic properties of biomacromolecules. This review discusses recent methodological development of NMR, their applications and some of the remaining challenges. Major Conclusions Although a major drawback of NMR is its difficulty in studying the dynamical ordering of larger biomolecular systems, current technologies have achieved considerable success in the structural analysis of substantially large proteins and biomolecular complexes over 1 MDa and have characterised a wide range of timescales across which biomolecular motion exists. While NMR is well suited to obtain local structure information in detail, it contributes valuable and unique information within hybrid approaches that combine complementary methodologies, including solution scattering and microscopic techniques. General Significance For living systems, the dynamic assembly and disassembly of macromolecular complexes is of utmost importance for cellular homeostasis and, if dysregulated, implied in human disease. It is thus instructive for the advancement of the study of the dynamical ordering to discuss the potential possibilities of solution NMR spectroscopy and its applications. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
PMID: 28847507 [PubMed - as supplied by publisher]
[NMR paper] New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy.
New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy.
Related Articles New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy.
J Mol Biol. 2015 Dec 18;
Authors: Kay LE
Abstract
In the past several decades solution NMR spectroscopy has emerged as a powerful technique for the study of the structure and dynamics of proteins, providing detailed insights into biomolecular function. Herein I provide a summary of two important areas of application, focusing on NMR studies of (i) supra-molecular...
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12-29-2015 08:05 PM
New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy
New Views of Functionally Dynamic Proteins by Solution NMR Spectroscopy
Publication date: Available online 19 December 2015
Source:Journal of Molecular Biology</br>
Author(s): Lewis E. Kay</br>
In the past several decades solution NMR spectroscopy has emerged as a powerful technique for the study of the structure and dynamics of proteins, providing detailed insights into biomolecular function. Herein I provide a summary of two important areas of application, focusing on NMR studies of (i) supra-molecular systems with aggregate molecular masses in the hundreds of...
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12-28-2015 12:26 AM
[NMR paper] 2Q NMR of (2)H2O ordering at solid interfaces.
2Q NMR of (2)H2O ordering at solid interfaces.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 2Q NMR of (2)H2O ordering at solid interfaces.
J Magn Reson. 2014 Jun;243:33-9
Authors: Krivokhizhina TV, Wittebort RJ
Abstract
Solvent ordering at an interface can be studied by multiple-quantum NMR. Quantitative studies of (2)H2O ordering require clean double-quantum (2Q) filtration and an analysis of 2Q buildup curves that accounts for...
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10-20-2015 09:44 PM
[NMR paper] In-Cell NMR and EPR Spectroscopy of Biomacromolecules.
In-Cell NMR and EPR Spectroscopy of Biomacromolecules.
In-Cell NMR and EPR Spectroscopy of Biomacromolecules.
Angew Chem Int Ed Engl. 2014 Jul 28;
Authors: Hänsel R, Luh LM, Corbeski I, Trantirek L, Dötsch V
Abstract
The dream of cell biologists is to be able to watch biological macromolecules perform their duties in the intracellular environment of live cells. Ideally, the observation of both the location and the conformation of these macromolecules with biophysical techniques is desired. The development of many fluorescence...
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04-06-2014 02:46 PM
[NMR paper] Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
J Biomol NMR. 2013 Aug 24;
Authors: Bernard D, Bédard M, Bilodeau J, Lavigne P
Abstract
Myc-interacting zinc finger protein-1 (Miz-1) is a BTB/POZ transcription factor that activates the...
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08-27-2013 11:10 PM
[NMR paper] NMR Spectroscopy on Domain Dynamics in Biomacromolecules.
NMR Spectroscopy on Domain Dynamics in Biomacromolecules.
Related Articles NMR Spectroscopy on Domain Dynamics in Biomacromolecules.
Prog Biophys Mol Biol. 2013 May 15;
Authors: Shapiro YE
Abstract
Domain dynamics in biomacromolecules is currently an area of intense research because of its importance for understanding the huge quantity of available data relating the structure and function of proteins and nucleic acids. Control of structural flexibility is essential for the proper functioning of the biomacromolecules. Biophysical...
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05-21-2013 02:34 PM
[Question from NMRWiki Q&A forum] Varian FIDs ordering: Inner and outer loop in the sequence(Rance-Kay & States)?
Varian FIDs ordering: Inner and outer loop in the sequence(Rance-Kay & States)?
Dear all,
I am new to NMR and I have difficulty understanding the ordering of FIDs, e.g. if an experiment uses both Rance-Kay and States, there will be loops(outer/inner) which need to be taken care during data processing. I don't completely understand how FIDs(indirect dimension) are stored and in what order. In a pulse sequnece, what an inner or outer loop corresponds to?
Check if somebody has answered this question on NMRWiki QA forum