Related Articles(1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.
Sci Rep. 2016;6:27851
Authors: Ravera E, Cerofolini L, Martelli T, Louka A, Fragai M, Luchinat C
Abstract
Proton-detection in solid-state NMR, enabled by high magnetic fields (>18 T) and fast magic angle spinning (>50 kHz), allows for the acquisition of traditional (1)H-(15)N experiments on systems that are too big to be observed in solution. Among those, proteins entrapped in a bioinspired silica matrix are an attractive target that is receiving a large share of attention. We demonstrate that (1)H-detected SSNMR provides a novel approach to the rapid assessment of structural integrity in proteins entrapped in bioinspired silica.
Studyingthe Conformation of a Silaffin-Derived PentalysinePeptide Embedded in Bioinspired Silica using Solution and DynamicNuclear Polarization Magic-Angle Spinning NMR
Studyingthe Conformation of a Silaffin-Derived PentalysinePeptide Embedded in Bioinspired Silica using Solution and DynamicNuclear Polarization Magic-Angle Spinning NMR
Yasmin Geiger, Hugo E. Gottlieb, U?mit Akbey, Hartmut Oschkinat and Gil Goobes
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b07809/20160419/images/medium/ja-2015-07809a_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b07809
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/T8sbiifgCd8
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[NMR paper] Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and DNP MAS NMR.
Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and DNP MAS NMR.
Related Articles Studying the Conformation of a Silaffin-Derived Pentalysine Peptide Embedded in Bioinspired Silica using Solution and DNP MAS NMR.
J Am Chem Soc. 2015 Oct 9;
Authors: Geiger Y, Gottlieb HE, Akbey Ü, Oschkinat H, Goobes G
Abstract
Smart materials are created in nature at interfaces between biomolecules and solid materials. The ability to probe the structure of functional peptides...
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10-10-2015 06:47 PM
[NMR paper] NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins.
NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins.
J Magn Reson. 2015 Apr;253:60-70
Authors: Ravera E, Schubeis T, Martelli T, Fragai M, Parigi G, Luchinat C
Abstract
Resolution and sensitivity in solid state NMR (SSNMR) can rival the results achieved by solution NMR, and even...
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NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins
NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins
Publication date: April 2015
Source:Journal of Magnetic Resonance, Volume 253</br>
Author(s): Enrico Ravera , Tobias Schubeis , Tommaso Martelli , Marco Fragai , Giacomo Parigi , Claudio Luchinat</br>
Resolution and sensitivity in solid state NMR (SSNMR) can rival the results achieved by solution NMR, and even outperform them in the case of large systems. However, several factors affect the spectral quality in SSNMR samples, and not all systems turn out to be equally...
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03-20-2015 01:48 AM
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy
Abstract Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the...
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09-20-2012 06:06 AM
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 20;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
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Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 14;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
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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...
(1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.
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