Publication date: April 2015 Source:Journal of Magnetic Resonance, Volume 253
Author(s): Christopher L. Suiter , Caitlin M. Quinn , Manman Lu , Guangjin Hou , Huilan Zhang , Tatyana Polenova
The negative global impact of the AIDS pandemic is well known. In this perspective article, the utility of magic angle spinning (MAS) NMR spectroscopy to answer pressing questions related to the structure and dynamics of HIV-1 protein assemblies is examined. In recent years, MAS NMR has undergone major technological developments enabling studies of large viral assemblies. We discuss some of these evolving methods and technologies and provide a perspective on the current state of MAS NMR as applied to the investigations into structure and dynamics of HIV-1 assemblies of CA capsid protein and of Gag maturation intermediates. Graphical abstract
[NMR paper] Information-driven modeling of large macromolecular assemblies using NMR data.
Information-driven modeling of large macromolecular assemblies using NMR data.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Information-driven modeling of large macromolecular assemblies using NMR data.
J Magn Reson. 2014 Apr;241:103-14
Authors: van Ingen H, Bonvin AM
Abstract
Availability of high-resolution atomic structures is one of the prerequisites for a mechanistic understanding of biomolecular function. This atomic...
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Magic AngleSpinning NMR Reveals Sequence-DependentStructural Plasticity, Dynamics, and the Spacer Peptide 1 Conformationin HIV-1 Capsid Protein Assemblies
Magic AngleSpinning NMR Reveals Sequence-DependentStructural Plasticity, Dynamics, and the Spacer Peptide 1 Conformationin HIV-1 Capsid Protein Assemblies
Yun Han, Guangjin Hou, Christopher L. Suiter, Jinwoo Ahn, In-Ja L. Byeon, Andrew S. Lipton, Sarah Burton, Ivan Hung, Peter L. Gor?kov, Zhehong Gan, William Brey, David Rice, Angela M. Gronenborn and Tatyana Polenova
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja406907h/aop/images/medium/ja-2013-06907h_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja406907h...
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[NMR paper] Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
Magic Angle Spinning NMR Reveals Sequence-Dependent Structural Plasticity, Dynamics, and the Spacer Peptide 1 Conformation in HIV-1 Capsid Protein Assemblies.
J Am Chem Soc. 2013 Oct 28;
Authors: Han Y, Hou G, Suiter CL, Ahn J, Byeon IJ, Lipton AS, Burton SD, Hung I, Gor'kov PL, Gan Z, Brey WW, Rice D, Gronenborn AM, Polenova TE
Abstract
A key stage in HIV-1 maturation towards...
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10-30-2013 10:44 AM
[NMR paper] Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Acc Chem Res. 2013 Feb 13;
Authors: Yan S, Suiter CL, Hou G, Zhang H, Polenova T
Abstract
In living organisms, biological molecules often organize into multicomponent complexes. Such assemblies consist of various proteins and carry out essential functions, ranging from cell division, transport, and energy transduction to catalysis, signaling, and viral...
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02-14-2013 02:37 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 systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies.
J Biomol NMR. 2011 May 29;
Authors: Amero C, Asunción Durá M, Noirclerc-Savoye M, Perollier A, Gallet B, Plevin MJ, Vernet T, Franzetti B, Boisbouvier J
Obtaining sequence-specific assignments remains a major bottleneck in solution NMR investigations of supramolecular structure, dynamics and interactions. Here we demonstrate that resonance...
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[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.
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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...
MAS NMR of HIV-1 protein assemblies
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