Publication date: April 2015 Source:Journal of Magnetic Resonance, Volume 253
Author(s): Christopher P. Jaroniec
Paramagnetism-based nuclear pseudocontact shifts and spin relaxation enhancements contain a wealth of information in solid-state NMR spectra about electron–nucleus distances on the ~20Å length scale, far beyond that normally probed through measurements of nuclear dipolar couplings. Such data are especially vital in the context of structural studies of proteins and other biological molecules that suffer from a sparse number of experimentally-accessible atomic distances constraining their three-dimensional fold or intermolecular interactions. This perspective provides a brief overview of the recent developments and applications of paramagnetic magic-angle spinning NMR to biological systems, with primary focus on the investigations of metalloproteins and natively diamagnetic proteins modified with covalent paramagnetic tags. Graphical abstract
[NMR paper] Temperature-Resistant Bicelles for Structural Studies by Solid-State NMR Spectroscopy.
Temperature-Resistant Bicelles for Structural Studies by Solid-State NMR Spectroscopy.
Temperature-Resistant Bicelles for Structural Studies by Solid-State NMR Spectroscopy.
Langmuir. 2015 Jan 7;
Authors: Yamamoto K, Pearcy P, Lee D, Yu C, Im S, Waskell LA, Ramamoorthy A
Abstract
Three-dimensional structure determination of membrane proteins is important to fully understand their biological functions. However, obtaining a high-resolution structure has been a major challenge mainly due to the difficulties in retaining the native...
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[NMR paper] Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.
Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.
Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.
J Biomol NMR. 2014 Nov 29;
Authors: Sengupta I, Gao M, Arachchige RJ, Nadaud PS, Cunningham TF, Saxena S, Schwieters CD, Jaroniec CP
Abstract
Paramagnetic relaxation enhancements (PREs) are a rich source of structural information in protein solid-state NMR spectroscopy. Here we...
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Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag
Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag
Abstract
Paramagnetic relaxation enhancements (PREs) are a rich source of structural information in protein solid-state NMR spectroscopy. Here we demonstrate that PRE measurements in natively diamagnetic proteins are facilitated by a thiol-reactive compact, cyclen-based, high-affinity Cu2+ binding tag, 1--1,4,7,10-tetraazacyclododecane (TETAC), that overcomes the key shortcomings associated with the use of larger, more flexible...
[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.
Related Articles 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.
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] Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Related Articles Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
J Am Chem Soc. 2004 Dec 1;126(47):15320-1
Authors: Lemaître V, de Planque MR, Howes AP, Smith ME, Dupree R, Watts A
We report the first example of 17O NMR spectra from a selectively labeled transmembrane peptide, 17O--WALP23, as a lyophilized powder and incorporated in hydrated phospholipid vesicles. It is shown that at high magnetic field it is feasible to apply...
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[NMR paper] Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
Related Articles Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy.
Annu Rev Phys Chem. 2003;54:531-71
Authors: Drobny GP, Long JR, Karlsson T, Shaw W, Popham J, Oyler N, Bower P, Stringer J, Gregory D, Mehta M, Stayton PS
Proteins directly control the nucleation and growth of biominerals, but the details of molecular recognition at the protein-biomineral interface remain poorly understood. The elucidation of recognition...
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Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phosph
Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers.
J Magn Reson. 2010 Aug 24;
Authors: Chu S, Maltsev S, Emwas AH, Lorigan GA
A new approach for determining the membrane immersion depth of a spin-labeled probe has been developed using paramagnetic relaxation enhancement (PRE)...
Structural studies of proteins by paramagnetic solid-state NMR spectroscopy
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