Pf1 bacteriophage hydration by magic angle spinning solid-state NMR.
J Chem Phys. 2014 Dec 14;141(22):22D533
Authors: Sergeyev IV, Bahri S, Day LA, McDermott AE
Abstract
High resolution two- and three-dimensional heteronuclear correlation spectroscopy ((1)H-(13)C, (1)H-(15)N, and (1)H-(13)C-(13)C HETCOR) has provided a detailed characterization of the internal and external hydration water of the Pf1 virion. This long and slender virion (2000 nm × 7 nm) contains highly stretched DNA within a capsid of small protein subunits, each only 46 amino acid residues. HETCOR cross-peaks have been unambiguously assigned to 25 amino acids, including most external residues 1-21 as well as residues 39-40 and 43-46 deep inside the virion. In addition, the deoxyribose rings of the DNA near the virion axis are in contact with water. The sets of cross-peaks to the DNA and to all 25 amino acid residues were from the same hydration water (1)H resonance; some of the assigned residues do not have exchangeable side-chain protons. A mapping of the contacts onto structural models indicates the presence of water "tunnels" through a highly hydrophobic region of the capsid. The present results significantly extend and modify results from a lower resolution study, and yield a comprehensive hydration surface map of Pf1. In addition, the internal water could be distinguished from external hydration water by means of paramagnetic relaxation enhancement. The internal water population may serve as a conveniently localized magnetization reservoir for structural studies.
[NMR paper] Recent advances in magic angle spinning solid state NMR of membrane proteins.
Recent advances in magic angle spinning solid state NMR of membrane proteins.
Recent advances in magic angle spinning solid state NMR of membrane proteins.
Prog Nucl Magn Reson Spectrosc. 2014 Oct;82C:1-26
Authors: Wang S, Ladizhansky V
Abstract
Membrane proteins mediate many critical functions in cells. Determining their three-dimensional structures in the native lipid environment has been one of the main objectives in structural biology. There are two major NMR methodologies that allow this objective to be accomplished....
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Recent advances in magic angle spinning solid state NMR of membrane proteins
From The DNP-NMR Blog:
Recent advances in magic angle spinning solid state NMR of membrane proteins
Wang, S. and V. Ladizhansky, Recent advances in magic angle spinning solid state NMR of membrane proteins. Prog. NMR. Spec., 2014. 82(0): p. 1-26.
http://www.sciencedirect.com/science/article/pii/S0079656514000478
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Recent advances in magic angle spinning solid state NMR of membrane proteins
Recent advances in magic angle spinning solid state NMR of membrane proteins
Publication date: Available online 26 July 2014
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Shenlin Wang , Vladimir Ladizhansky</br>
Membrane proteins mediate many critical functions in cells. Determining their three-dimensional structures in the native lipid environment has been one of the main objectives in structural biology. There are two major NMR methodologies that allow this objective to be accomplished. Oriented sample NMR, which can be applied to...
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07-27-2014 01:05 AM
[NMR paper] Solid-state NMR Spectra of lipid-anchored Proteins under Magic Angle Spinning.
Solid-state NMR Spectra of lipid-anchored Proteins under Magic Angle Spinning.
Related Articles Solid-state NMR Spectra of lipid-anchored Proteins under Magic Angle Spinning.
J Phys Chem B. 2014 Feb 11;
Authors: Nomura K, Harada E, Sugase K, Shimamoto K
Abstract
Solid-state NMR is a promising tool for elucidating membrane-related biological phenomena. We achieved the measurement of high-resolution solid-state NMR spectra for a lipid-anchored protein embedded in lipid bilayers under magic angle spinning (MAS). To date, solid-state NMR...
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[NMR paper] Magic-angle spinning solid-state multinuclear NMR on low-field instrumentation.
Magic-angle spinning solid-state multinuclear NMR on low-field instrumentation.
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J Magn Reson. 2013 Nov 1;238C:20-25
Authors: Sørensen MK, Bakharev O, Jensen O, Jakobsen HJ, Skibsted J, Nielsen NC
Abstract
Mobile and cost-effective NMR spectroscopy exploiting low-field permanent magnets is a field of tremendous development with obvious applications for arrayed large scale analysis, field work, and industrial screening. So far such...
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[NMR paper] Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
Biomolecular magic-angle spinning solid-state NMR: recent methods and applications.
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Curr Opin Biotechnol. 2013 Mar 4;
Authors: Goldbourt A
Abstract
The link of structure and dynamics of biomolecules and their complexes to their function and to many cellular processes has driven the quest for their detailed characterization by a variety of biophysical techniques. Magic-angle spinning solid-state nuclear magnetic resonance spectroscopy...
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[NMR paper] Magic angle spinning solid-state NMR spectroscopy for structural studies of protein i
Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
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J Am Chem Soc. 2004 Dec 22;126(50):16608-20
Authors: Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V,...
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[NMR paper] Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscop
Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
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Nature. 2002 Nov 7;420(6911):98-102
Authors: Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H
The determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not...
Pf1 bacteriophage hydration by magic angle spinning solid-state NMR.
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