Publication date: May 2016 Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volumes 94–95
Author(s): Suliman Barhoum, Swomitra Palit, Anand Yethiraj
Label-free methods to obtain hydrodynamic size from diffusion measurements are desirable in environments that contain multiple macromolecular species at a high total concentration: one example is the crowded cellular environment. In complex, multi-species macromolecular environments – in this article, we feature aqueous systems involving polymers, surfactants and proteins – the link between dynamics and size is harder to unpack due to macromolecular crowding and confinement. In this review, we demonstrate that the pulsed-field gradient NMR technique, with its spectral separation of different chemical components, is ideal for studying the dynamics of the entire system simultaneously and without labelling, in a wide range of systems. The simultaneous measurement of the dynamics of multiple components allows for internal consistency checks and enables quantitative statements about the link between macromolecular dynamics, size, complex formation and crowding in soft materials. Graphical abstract
Understanding macromolecular crowding is critical for quantitative cell biology - SPIE Newsroom
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SPIE Newsroom
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Understanding macromolecular crowding is critical for quantitative cell biology
SPIE Newsroom
In the past, nuclear magnetic resonance (NMR) has been used to study protein-crowded environments and to investigate the translational and rotational diffusion of chymotrypsin inhibitor 2 in crowded environments. It was found that the heterogeneity of ...
Understanding macromolecular crowding is critical for...
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12-15-2015 07:47 AM
Understanding macromolecular crowding is critical for quantitative cell biology - SPIE Newsroom
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SPIE Newsroom
<img alt="" height="1" width="1">
Understanding macromolecular crowding is critical for quantitative cell biology
SPIE Newsroom
In the past, nuclear magnetic resonance (NMR) has been used to study protein-crowded environments and to investigate the translational and rotational diffusion of chymotrypsin inhibitor 2 in crowded environments. It was found that the heterogeneity of ...
Understanding macromolecular crowding is critical for...
nmrlearner
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12-12-2015 03:39 AM
[NMR paper] Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Apr 29;
Authors: Scanu S, Förster J, Ullmann GM, Ubbink M
Abstract
Protein complex formation is thought to be at least a two-step process, in which the active complex is preceded by the formation of an encounter complex....
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05-01-2013 11:46 AM
Translational Diffusion of Macromolecular Assemblies Measured Using Transverse-Relaxation-Optimized Pulsed Field Gradient NMR
Translational Diffusion of Macromolecular Assemblies Measured Using Transverse-Relaxation-Optimized Pulsed Field Gradient NMR
Reto Horst, Arthur L. Horwich and Kurt Wu?thrich
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206531c/aop/images/medium/ja-2011-06531c_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206531c
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09-26-2011 06:54 PM
Translational diffusion of macromolecular assemblies measured using transverse relaxation-optimized PFG-NMR.
Translational diffusion of macromolecular assemblies measured using transverse relaxation-optimized PFG-NMR.
Translational diffusion of macromolecular assemblies measured using transverse relaxation-optimized PFG-NMR.
J Am Chem Soc. 2011 Sep 16;
Authors: Horst R, Horwich AL, Wüthrich K
Abstract
ABSTRACT In structural biology, pulsed field gradient (PFG) NMR for characterization of size and hydrodynamic parameters of macromolecular solutes has the advantage over other techniques that the measurements can be recorded with identical solution...
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09-17-2011 08:21 PM
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
Proteins. 2010 Dec 13;
Authors: Martorell G, Adrover M, Kelly G, Temussi PA, Pastore A
In vitro studies of biological macromolecules are usually performed in dilute, buffered solutions containing one or just a few different biological macromolecules. Under these conditions, the interactions among molecules are diffusion limited. On the contrary, in living systems,...
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02-22-2011 10:40 PM
[NMR paper] Slow diffusion of macromolecular assemblies by a new pulsed field gradient NMR method
Slow diffusion of macromolecular assemblies by a new pulsed field gradient NMR method.
Related Articles Slow diffusion of macromolecular assemblies by a new pulsed field gradient NMR method.
J Am Chem Soc. 2003 Mar 5;125(9):2541-5
Authors: Ferrage F, Zoonens M, Warschawski DE, Popot JL, Bodenhausen G
The translational diffusion coefficient of an integral membrane protein/surfactant complex has been measured using a novel pulsed field gradient NMR method. In this new approach, the information about the localization of the molecules is...
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11-24-2010 09:01 PM
[NMR paper] A novel approach for assessing macromolecular complexes combining soft-docking calcul
A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data.
Related Articles A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data.
Protein Sci. 2001 Oct;10(10):2131-7
Authors: Morelli XJ, Palma PN, Guerlesquin F, Rigby AC
We present a novel and efficient approach for assessing protein-protein complex formation, which combines ab initio docking calculations performed with the protein docking algorithm BiGGER and chemical shift perturbation data...
Diffusion NMR studies of macromolecular complex formation, crowding and confinement in soft materials
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