[NMR paper] Interaction of bovine serum albumin (BSA) with novel gemini surfactants studied by synchrotron radiation scattering (SR-SAXS), circular dichroism (CD), and nuclear magnetic resonance (NMR).
Interaction of bovine serum albumin (BSA) with novel gemini surfactants studied by synchrotron radiation scattering (SR-SAXS), circular dichroism (CD), and nuclear magnetic resonance (NMR).
Related ArticlesInteraction of bovine serum albumin (BSA) with novel gemini surfactants studied by synchrotron radiation scattering (SR-SAXS), circular dichroism (CD), and nuclear magnetic resonance (NMR).
J Phys Chem B. 2014 Jul 24;118(29):8652-61
Authors: Gospodarczyk W, Szutkowski K, Kozak M
Abstract
The interaction of three dicationic (gemini) surfactants-3,3'-[1,6-(2,5-dioxahexane)]bis(1-dodecylimidazolium) chloride (oxyC2), 3,3'-[1,16-(2,15-dioxahexadecane)]bis(1-dodecylimidazolium) chloride (oxyC12), and 1,4-bis(butane)imidazole-1-yl-3-dodecylimidazolium chloride (C4)--with bovine serum albumin (BSA) has been studied by the use of small-angle X-ray scattering (SAXS), circular dichroism (CD), and (1)H nuclear magnetic resonance diffusometry. The results of CD studies show that the conformation of BSA was changed dramatically in the presence of all studied surfactants. The greater decrease (from 56 to 24%) in the ?-helical structure of BSA was observed for oxyC2 surfactant. The radii of gyration estimated from SAXS data varied between 3 and 26 nm for the BSA/oxyC2 and BSA/oxyC12 systems. The hydrodynamic radius of the BSA/surfactant system estimated from NMR diffusometry varies between 5 and 11 nm for BSA/oxyC2 and 5 and 8 nm for BSA/oxyC12.
[NMR paper] Insoluble Protein Characterization by Circular Dichroism (CD) Spectroscopy and Nuclear Magnetic Resonance (NMR).
Insoluble Protein Characterization by Circular Dichroism (CD) Spectroscopy and Nuclear Magnetic Resonance (NMR).
Insoluble Protein Characterization by Circular Dichroism (CD) Spectroscopy and Nuclear Magnetic Resonance (NMR).
Methods Mol Biol. 2015;1258:371-85
Authors: Goyal S, Qin H, Lim L, Song J
Abstract
Besides misfolded proteins, which still retain the capacity to fold into uniquely defined structures but are misled to "off-pathway" aggregation, there exists a group of proteins which are unrefoldable and insoluble in...
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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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[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...
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01-28-2014 11:53 AM
Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
1 March 2012
Publication year: 2012
Source:Journal of Colloid and Interface Science, Volume 369, Issue 1</br>
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Gemini surfactants have two polar head groups and two hydrocarbon tails. Compared with conventional surfactants, geminis have much lower (?M vs. mM) critical micelle concentrations and possess slower (ms vs. ?s) monomer ? micelle kinetics. The structure of the gemini surfactants studied is ·2Br- where s =4, 5, or 6. Our objective is to reveal the effect...
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[NMR paper] An NMR and circular dichroism study of the interaction of thiocyanate with human and
An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Related Articles An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Biophys Chem. 2003 Dec 1;106(3):233-40
Authors: Sau AK, Currell D, Mazumdar S, Mitra S
The interaction of thiocyanate with human native and cross-linked...
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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...
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[NMR paper] Circular dichroic and 1H-NMR studies on the aged form of bovine plasma albumin.
Circular dichroic and 1H-NMR studies on the aged form of bovine plasma albumin.
Related Articles Circular dichroic and 1H-NMR studies on the aged form of bovine plasma albumin.
Int J Pept Protein Res. 1991 Sep;38(3):260-6
Authors: Era S, Kuwata K, Sogami M, Kato K, Watari H
Bovine plasma albumin (BPA) has 17 disulfide bonds and approximately one SH group at Cys-34 which catalyzes the intramolecular SH, S-S exchange reaction in the alkaline region at low ionic strength, resulting in the formation of the aged form (A-form). 1) Fractions of...
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[NMR paper] Circular dichroic and 1H-NMR studies on the aged form of bovine plasma albumin.
Circular dichroic and 1H-NMR studies on the aged form of bovine plasma albumin.
Related Articles Circular dichroic and 1H-NMR studies on the aged form of bovine plasma albumin.
Int J Pept Protein Res. 1991 Sep;38(3):260-6
Authors: Era S, Kuwata K, Sogami M, Kato K, Watari H
Bovine plasma albumin (BPA) has 17 disulfide bonds and approximately one SH group at Cys-34 which catalyzes the intramolecular SH, S-S exchange reaction in the alkaline region at low ionic strength, resulting in the formation of the aged form (A-form). 1) Fractions of...
Interaction of bovine serum albumin (BSA) with novel gemini surfactants studied by synchrotron radiation scattering (SR-SAXS), circular dichroism (CD), and nuclear magnetic resonance (NMR).
Linear Mode
