Conformational change of protein sodium dodecylsulfate complexes in solution: A study of dynamic light scattering

1982 ◽  
Vol 76 (8) ◽  
pp. 3866-3872 ◽  
Author(s):  
R. E. Tanner ◽  
B. Herpigny ◽  
S.‐H. Chen ◽  
C. K. Rha
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Conformational Change ◽  
Sodium Dodecylsulfate

scholarly journals DIAMETER OF SODIUM DI-(2-ETHYLHEXYL)PHOSPHATE AND SODIUM DODECYLSULFATE REVERSE MICROEMULSION DROPLETS: EXPERIMENTAL DATA AND CALCULATION METHODS

2021 ◽  
Vol 64 (2) ◽  
pp. 66-72
Author(s):  
Anastasia S. Polyakova ◽  
Nataliya M. Murashova
Keyword(s):  
Experimental Data ◽  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Water Content ◽  
Sodium Dodecyl ◽  
Sodium Dodecylsulfate ◽  
Water System ◽  
Surfactant Molecule ◽  
Reverse Microemulsion ◽  
Molar Ratio

The article is concerned with study of diameters of reverse microemulsion droplets depending on the water content in sodium bis-(2-ethylhexyl)phosphate – decane – water and sodium dodecylsulfate – butanol-1 – decane – water systems. Hydrodinamic diameters of microemulsion droplets were determined by the method of dynamic light scattering. It increases from 5.9 to 9.7 nm with an increase in the molar ratio of water and sodium bis-(2-ethylhexyl)phosphate from 5.0 to 20.0 in the sodium bis-(2-ethylhexyl)phosphate – decane – water microemulsion. Diameter of microemulsion droplets in the sodium dodecylsulfate – butanol-1 – decane – water system increases from 2.4 to 8.6 nm with an increase in the molar ratio of water and dodecylsulfate from 7.5 to 30.0. It was shown that the dependence of the diameter (d) on the water content (W) is linear. The applicability of the experimental data on the area per surfactant molecule at the "water-oil" interface and literature data on the values of molar volumes of microemulsion components to calculate the diameter of microemulsion droplets was analyzed. It was shown that the equation of the form d = kW + b is suitable for describing the dependence of the diameter of microemulsion droplets on the water content in the sodium dodecyl sulfate-butanol – 1-decane-water system. Parameters k and b of this equation are calculated using the value of the area per surfactant molecule at the "water-oil" interface, which can be obtained from experimental data on interfacial tension. Values of the diameter of microemulsion droplets calculated using the proposed equation differ by no more than 1 nm from the values obtained by dynamic light scattering. Values of the droplet diameter of microemulsion in the DEHPA – decane – water system calculated using this equation are underestimated by 1.0-2.5 nm relative to the experimental values, while the slope of the lines obtained from the experimental data and during the calculation is almost the same.

Thermostability of endo-1,4-β-xylanase II from Trichoderma reesei studied by electrospray ionization Fourier-transform ion cyclotron resonance MS, hydrogen/deuterium-exchange reactions and dynamic light scattering

2001 ◽  
Vol 356 (2) ◽  
pp. 453-460 ◽  
Author(s):  
Janne JÄNIS ◽  
Juha ROUVINEN ◽  
Matti LEISOLA ◽  
Ossi TURUNEN ◽  
Pirjo VAINIOTALO
Keyword(s):  
Fourier Transform ◽  
Transition Temperature ◽  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Conformational Change ◽  
Cyclotron Resonance ◽  
Enzymic Activity ◽  
Ion Cyclotron Resonance ◽  
Exchange Reactions ◽  
Hydrogen Deuterium

Endo-1,4-β-xylanase II (XYNII) from Trichoderma reesei is a 21kDa enzyme that catalyses the hydrolysis of xylan, the major plant hemicellulose. It has various applications in the paper, food and feed industries. Previous thermostability studies have revealed a significant decrease in enzymic activity of the protein at elevated temperatures in citrate buffer [Tenkanen, Puls and Poutanen (1992) Enzyme Microb. Technol. 14, 566–574]. Here, thermostability of XYNII was investigated using both conventional and nanoelectrospray ionization Fourier-transform ion cyclotron resonance MS and hydrogen/deuterium (H/D)-exchange reactions. In addition, dynamic light scattering (DLS) was used as a comparative method to observe possible changes in both tertiary and quaternary structures of the protein. We observed a significant irreversible conformational change and dimerization when the protein was exposed to heat. H/D exchange revealed two distinct monomeric protein populations in a narrow transition temperature region. The conformational change in both the water and buffered solutions occurred in the same temperature region where enzymic-activity loss had previously been observed. Approx. 10–30% of the protein was specifically dimerized when exposed to the heat treatment. However, adding methanol to the solution markedly lowered the transition temperature of conformational change as well as increased the dimerization up to 90%. DLS studies in water confirmed the change in conformation observed by electrospray ionization MS. We propose that the conformational change is responsible for the loss of enzymic activity at temperatures over 50°C and that the functioning of the active site in the enzyme is unfeasible in a new, more labile solution conformation.

scholarly journals Dynamic light scattering study of the conformational change of ovotransferrin induced by the binding of lanthanoid ions.

1990 ◽  
pp. 185-191 ◽  
Author(s):  
Noriyuki SASAKI ◽  
Hisashi HONDA ◽  
Hirofumi YAJIMA ◽  
Hiroyuki MOMOMI ◽  
Kaoru ICHIMURAK ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Conformational Change ◽  
Scattering Study

Dynamic light scattering from gels in a poor solvent

1978 ◽  
Vol 39 (9) ◽  
pp. 955-960 ◽  
Author(s):  
E. Geissler ◽  
A.M. Hecht
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Poor Solvent
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