Publication date: Available online 5 May 2017 Source:Archives of Biochemistry and Biophysics
Author(s): Chitra Narayanan, Khushboo Bafna, Louise D. Roux, Pratul K. Agarwal, Nicolas Doucet
Overwhelming evidence now illustrates the defining role of atomic-scale protein flexibility in biological events such as allostery, cell signaling, and enzyme catalysis. Over the years, spin relaxation nuclear magnetic resonance (NMR) has provided significant insights on the structural motions occurring on multiple time frames over the course of a protein life span. The present review article aims to illustrate to the broader community how this technique continues to shape many areas of protein science and engineering, in addition to being an indispensable tool for studying atomic-scale motions and functional characterization. Continuing developments in underlying NMR technology alongside software and hardware developments for complementary computational approaches now enable methodologies to routinely provide spatial directionality and structural representations traditionally harder to achieve solely using NMR spectroscopy. In addition to its well-established role in structural elucidation, we present recent examples that illustrate the combined power of selective isotope labeling, relaxation dispersion experiments, chemical shift analyses, and computational approaches for the characterization of conformational sub-states in proteins and enzymes. Graphical abstract
Modular 129Xe NMR biosensor for MRI applications [Biophysics and Computational Biology]
Modular 129Xe NMR biosensor for MRI applications
Rose, H. M., Witte, C., Rossella, F., Klippel, S., Freund, C., Schroder, L....
Date: 2014-08-12
Magnetic resonance imaging (MRI) is seriously limited when aiming for visualization of targeted contrast agents. Images are reconstructed from the weak diamagnetic properties of the sample and require an abundant molecule like water as the reporter. Micromolar to millimolar concentrations of conventional contrast agents are needed to generate image contrast,... Read More
PNAS:
Number: 32
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08-13-2014 07:49 AM
Protein dynamics from X-ray and NMR [Biophysics and Computational Biology]
Protein dynamics from X-ray and NMR
Fenwick, R. B., van den Bedem, H., Fraser, J. S., Wright, P. E....
Date: 2014-01-28
Detailed descriptions of atomic coordinates and motions are required for an understanding of protein dynamics and their relation to molecular recognition, catalytic function, and allostery. Historically, NMR relaxation measurements have played a dominant role in the determination of the amplitudes and timescales (picosecond–nanosecond) of bond vector fluctuations, whereas high-resolution X-ray... Read More
PNAS:
Number: 4
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01-29-2014 12:50 AM
[NMR paper] A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
Chembiochem. 2013 Jun 19;
Authors: Vallurupalli P, Bouvignies G, Kay LE
Abstract
Read the label: The NMR CEST experiment can be used to reconstruct spectra of sparsely populated, transiently formed protein conformers so long as...
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06-21-2013 01:10 PM
Computational approaches to the interpretation of NMR data for studying protein dynamics
Computational approaches to the interpretation of NMR data for studying protein dynamics
2 March 2012
Publication year: 2012
Source:Chemical Physics, Volume 396</br>
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Experimental studies of protein structure and dynamics with NMR provide the classical example of the power of theoretical approaches for the interpretation of experimental results. In this paper we review recent developments in experimental techniques extending the applicability of NMR to the study of protein structure and motion, and advances in the theoretical description.
Graphical abstract
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Current applications of 19F NMR to studies of protein structure and dynamics
Current applications of 19F NMR to studies of protein structure and dynamics
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 62</br>
Julianne L. Kitevski-LeBlanc, R. Scott Prosser</br>
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03-09-2012 09:16 AM
[NMR paper] Protein dynamics from solution NMR: theory and applications.
Protein dynamics from solution NMR: theory and applications.
Related Articles Protein dynamics from solution NMR: theory and applications.
Cell Biochem Biophys. 2003;37(3):187-211
Authors: Kempf JG, Loria JP
Solution nuclear magnetic resonance (NMR) spectroscopy is unique in its ability to elucidate the details of atomic-level structural and dynamical properties of biological macromolecules under native-like conditions. Recent advances in NMR techniques and protein sample preparation now allow comprehensive investigation of protein dynamics...
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11-24-2010 09:01 PM
Using NMR to study fast dynamics in proteins: methods and applications.
Using NMR to study fast dynamics in proteins: methods and applications.
Related Articles Using NMR to study fast dynamics in proteins: methods and applications.
Curr Opin Pharmacol. 2010 Oct 6;
Authors: Sapienza PJ, Lee AL
Proteins exist not as singular structures with precise coordinates, but rather as fluctuating bodies that move rapidly through an enormous number of conformational substates. These dynamics have important implications for understanding protein function and for structure-based drug design. NMR spectroscopy is particularly well...
Applications of NMR and computational methodologies to study protein dynamics
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