The effects of high concentrations of ionic liquid on GB1 protein structure and dynamics probed by high-resolution magic-angle-spinning NMR spectroscopy
The effects of high concentrations of ionic liquid on GB1 protein structure and dynamics probed by high-resolution magic-angle-spinning NMR spectroscopy
Publication date: Available online 11 August 2016
Source:Biochemistry and Biophysics Reports</br>
Author(s): Lisa Warner, Erica Gjersing, Shelby E. Follett, K. Wade Elliott, Sergei V. Dzyuba, Krisztina Varga</br>
Ionic liquids have great potential in biological applications and biocatalysis, as some ionic liquids can stabilize proteins and enhance enzyme activity, while others have the opposite effect....
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08-11-2016 07:03 PM
StructureElucidation of Mixed-Linker Zeolitic ImidazolateFrameworks by Solid-State 1H CRAMPS NMR Spectroscopy andComputational Modeling
StructureElucidation of Mixed-Linker Zeolitic ImidazolateFrameworks by Solid-State 1H CRAMPS NMR Spectroscopy andComputational Modeling
Krishna C. Jayachandrababu, Ross J. Verploegh, Johannes Leisen, Ryan C. Nieuwendaal, David S. Sholl and Sankar Nair
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b02754/20160602/images/medium/ja-2016-02754g_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02754
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-03-2016 03:35 AM
[NMR paper] Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
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J Mol Biol. 2014 Feb 12;
Authors: Sinnige T, Weingarth M, Renault M, Baker L, Tommassen J, Baldus M
Abstract
The outer membrane protein BamA is the key player in ?-barrel assembly in Gram-negative bacteria. Despite the availability of high-resolution crystal structures, the dynamic behavior of the transmembrane domain and...
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02-19-2014 12:07 AM
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
J Agric Food Chem. 2011 Jan 10;
Authors: Monogioudi E, Permi P, Filpponen I, Lienemann M, Li B, Argyropoulos D, Buchert J, Mattinen ML
Cross-linking of ?-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic...
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01-12-2011 11:11 AM
[NMR paper] Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
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J Am Chem Soc. 2005 Sep 7;127(35):12263-72
Authors: Vogel A, Katzka CP, Waldmann H, Arnold K, Brown MF, Huster D
The human N-ras protein binds to cellular membranes by insertion of two covalently bound posttranslational lipid modifications, which is crucial for its...
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12-01-2010 06:56 PM
[NMR paper] A solid-state NMR study of molecular mobility and phase separation in co-spray-dried
A solid-state NMR study of molecular mobility and phase separation in co-spray-dried protein-sugar particles.
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Eur J Pharm Sci. 2005 May;25(1):105-12
Authors: Suihko EJ, Forbes RT, Apperley DC
Molecular mobility and physical form of co-spray-dried sugar-lysozyme formulations were evaluated. Co-spray-dried trehalose:lysozyme and sucrose:lysozyme formulations in 1:9, 1:1 and 9:1 ratios (w:w) were stored at 0% RH and 75%...
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11-25-2010 08:21 PM
[NMR paper] Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy wit
Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.
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Chembiochem. 2004 Apr 2;5(4):467-73
Authors: Hilty C, Wider G, Fernández C, Wüthrich K
For solution NMR studies of the structure and function of membrane proteins, these macromolecules have to be reconstituted and solubilized in detergent micelles. Detailed characterization of the mixed...
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11-24-2010 09:51 PM
[NMR paper] A solid-state NMR study of protein mobility in lyophilized protein-sugar powders.
A solid-state NMR study of protein mobility in lyophilized protein-sugar powders.
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J Pharm Sci. 2002 Apr;91(4):943-51
Authors: Lam YH, Bustami R, Phan T, Chan HK, Separovic F
The molecular mobility of protein in lyophilized lysozyme-sugar systems stored at different relative humidities was studied using solid-state NMR. Relaxation measurements, T(1) of high-frequency (MHz), and T(1rho), of low-frequency (kHz) motions, were performed on lysozyme...