Related ArticlesUbiquitin immobilized on mesoporous MCM41 silica surfaces - Analysis by solid-state NMR with biophysical and surface characterization.
Biointerphases. 2017 May 31;12(2):02D414
Authors: Adiram-Filiba N, Schremer A, Ohaion E, Nadav-Tsubery M, Lublin-Tennenbaum T, Keinan-Adamsky K, Goobes G
Abstract
Deriving the conformation of adsorbed proteins is important in the assessment of their functional activity when immobilized. This has particularly important bearings on the design of contemporary and new encapsulated enzyme-based drugs, biosensors, and other bioanalytical devices. Solid-state nuclear magnetic resonance (NMR) measurements can expand our molecular view of proteins in this state and of the molecular interactions governing protein immobilization on popular biocompatible surfaces such as silica. Here, the authors study the immobilization of ubiquitin on the mesoporous silica MCM41 by NMR and other techniques. Protein molecules are shown to bind efficiently at pH 5 through electrostatic interactions to individual MCM41 particles, causing their agglutination. The strong attraction of ubiquitin to MCM41 surface is given molecular context through evidence of proximity of basic, carbonyl and polar groups on the protein to groups on the silica surface using NMR measurements. The immobilized protein exhibits broad peaks in two-dimensional (13)C dipolar-assisted rotational resonance spectra, an indication of structural multiplicity. At the same time, cross-peaks related to Tyr and Phe sidechains are missing due to motional averaging. Overall, the favorable adsorption of ubiquitin to MCM41 is accompanied by conformational heterogeneity and by a major loss of motional degrees of freedom as inferred from the marked entropy decrease. Nevertheless, local motions of the aromatic rings are retained in the immobilized state.
Spatial distribution of organic functional groups supported on mesoporous silica nanoparticles: a study by conventional and DNP-enhanced 29Si solid-state NMR #DNPNMR
From The DNP-NMR Blog:
Spatial distribution of organic functional groups supported on mesoporous silica nanoparticles: a study by conventional and DNP-enhanced 29Si solid-state NMR #DNPNMR
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Kobayashi, T., et al., Spatial distribution of organic functional groups supported on mesoporous silica nanoparticles: a study by conventional and DNP-enhanced 29Si solid-state NMR. Phys. Chem. Chem. Phys., 2017. 19(3): p. 1781-1789.
https://www.ncbi.nlm.nih.gov/pubmed/28058422
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03-01-2017 05:04 PM
[NMR paper] (1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.
(1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif 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...
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06-10-2016 10:49 PM
[NMR paper] Solid-state NMR studies of proteins immobilized on inorganic surfaces.
Solid-state NMR studies of proteins immobilized on inorganic surfaces.
Solid-state NMR studies of proteins immobilized on inorganic surfaces.
Solid State Nucl Magn Reson. 2014 Oct 29;
Authors: Shaw WJ
Abstract
Solid state NMR is the primary tool for studying the quantitative, site-specific structure, orientation, and dynamics of biomineralization proteins under biologically relevant conditions. Two calcium phosphate proteins, statherin (43 amino acids) and leucine rich amelogenin protein (LRAP; 59 amino acids), have been studied...
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12-04-2014 05:36 PM
Solid-state NMR studies of proteins immobilized on inorganic surfaces
Solid-state NMR studies of proteins immobilized on inorganic surfaces
Publication date: Available online 29 October 2014
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Wendy Shaw</br>
Solid state NMR is the primary tool for studying the quantitative, site-specific structure, orientation, and dynamics of biomineralization proteins under biologically relevant conditions. Two calcium phosphate proteins, statherin (43 amino acids) and leucine rich amelogenin protein (LRAP; 59 amino acids), have been studied in depth and have different dynamic properties...
Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
From The DNP-NMR Blog:
Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
Kobayashi, T., et al., Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials. Phys Chem Chem Phys, 2013. 15(15): p. 5553-62.
http://www.ncbi.nlm.nih.gov/pubmed/23459985
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04-17-2013 08:15 PM
Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
From the The DNP-NMR Blog:
Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials
Kobayashi, T., et al., Analysis of sensitivity enhancement by dynamic nuclear polarization in solid-state NMR: a case study of functionalized mesoporous materials. Phys Chem Chem Phys, 2013. 15(15): p. 5553-62.
http://www.ncbi.nlm.nih.gov/pubmed/23459985
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04-15-2013 08:52 AM
Nature and Structure of Aluminum Surface Sites Grafted on Silica from a Combination of High-Field Aluminum-27 Solid-State NMR Spectroscopy and First-Principles Calculations
Nature and Structure of Aluminum Surface Sites Grafted on Silica from a Combination of High-Field Aluminum-27 Solid-State NMR Spectroscopy and First-Principles Calculations
Rachel Nathaniel Kerber, Anthony Kermagoret, Emmanuel Callens, Pierre Florian, Dominique Massiot, Anne Lesage, Christophe Cope?ret, Franc?oise Delbecq, Xavier Rozanska and Philippe Sautet
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3008566/aop/images/medium/ja-2012-008566_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3008566
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