DNP-enhanced MAS NMR of bovine serum albumin sediments and solutions
From The DNP-NMR Blog:
DNP-enhanced MAS NMR of bovine serum albumin sediments and solutions
Ravera, E., et al., DNP-enhanced MAS NMR of bovine serum albumin sediments and solutions. J Phys Chem B, 2014. 118(11): p. 2957-65.
http://www.ncbi.nlm.nih.gov/pubmed/24460530
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DNP-Enhanced MAS NMR of Bovine Serum Albumin Sediments and Solutions
From The DNP-NMR Blog:
DNP-Enhanced MAS NMR of Bovine Serum Albumin Sediments and Solutions
Ravera, E., et al., DNP-Enhanced MAS NMR of Bovine Serum Albumin Sediments and Solutions. J Phys Chem B, 2014.
http://www.ncbi.nlm.nih.gov/pubmed/24460530
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03-05-2014 11:57 PM
[NMR paper] DNP-enhanced MAS NMR of Bovine Serum Albumin Sediments and Solutions.
DNP-enhanced MAS NMR of Bovine Serum Albumin Sediments and Solutions.
DNP-enhanced MAS NMR of Bovine Serum Albumin Sediments and Solutions.
J Phys Chem B. 2014 Jan 24;
Authors: Ravera E, Corzilius B, Michaelis VK, Luchinat C, Griffin RG, Bertini I
Abstract
Protein sedimentation sans cryoprotection is a new approach to magic angle spinning (MAS) and dynamic nuclear polarization (DNP) nuclear magnetic resonance (NMR) spectroscopy of proteins. It increases the sensitivity of the experiments by a factor of ~4.5 in comparison to the...
[NMR paper] Determination of molecular mobility of lyophilized bovine serum albumin and gamma-glo
Determination of molecular mobility of lyophilized bovine serum albumin and gamma-globulin by solid-state 1H NMR and relation to aggregation-susceptibility.
Related Articles Determination of molecular mobility of lyophilized bovine serum albumin and gamma-globulin by solid-state 1H NMR and relation to aggregation-susceptibility.
Pharm Res. 1996 Jun;13(6):926-30
Authors: Yoshioka S, Aso Y, Kojima S
PURPOSE: Feasibility of solid-state 1H NMR for determining the mobility of protein molecules in lyophilized cakes was considered. The mobility in...
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08-22-2010 02:27 PM
[NMR paper] Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiple
Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study.
Biochemistry. 1996 Jan 9;35(1):340-7
Authors: Avdulov NA, Chochina SV, Daragan VA, Schroeder F, Mayo KH, Wood WG
Molecular mechanisms of ethanol interaction with proteins are not well-understood. In the present study, direct...
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[NMR paper] The influence of hydration on the conformation of bovine serum albumin studied by sol
The influence of hydration on the conformation of bovine serum albumin studied by solid-state 13C-NMR spectroscopy.
Related Articles The influence of hydration on the conformation of bovine serum albumin studied by solid-state 13C-NMR spectroscopy.
Biopolymers. 1993 Dec;33(12):1871-6
Authors: Gregory RB, Gangoda M, Gilpin RK, Su W
13C proton-decoupled cross-polarization magic-angle spinning nmr spectra of bovine serum albumin are reported as a function of hydration. Increases in hydration level enhance the resolution of the peak centered at...