Enthalpy of interaction between some globular proteins and sodium n-dodecyl sulphate in aqueous solution

1974 ◽  
Vol 70 (0) ◽  
pp. 1306 ◽  
Author(s):  
Edward Tipping ◽  
Malcolm N. Jones ◽  
Henry A. Skinner
Keyword(s):  
Aqueous Solution ◽  
Globular Proteins ◽  
Enthalpy Of Interaction

The unfolding effects on the protein hydration shell and partial molar volume: a computational study

2016 ◽  
Vol 18 (40) ◽  
pp. 28175-28182 ◽  
Author(s):  
Sara Del Galdo ◽  
Andrea Amadei
Keyword(s):  
Aqueous Solution ◽  
Computational Analysis ◽  
Computational Study ◽  
Hydration Shell ◽  
Partial Molar Volumes ◽  
Globular Proteins ◽  
Protein Hydration ◽  
Native Protein ◽  
Unfolded State ◽  
Protein Hydration Shell

In this paper we apply the computational analysis recently proposed by our group to characterize the solvation properties of a native protein in aqueous solution, and to four model aqueous solutions of globular proteins in their unfolded states thus characterizing the protein unfolded state hydration shell and quantitatively evaluating the protein unfolded state partial molar volumes.

Interactions in globular proteins with polyampholyte: coacervation route for protein separation

RSC Advances ◽  
2015 ◽  
Vol 5 (18) ◽  
pp. 13579-13589 ◽  
Author(s):  
Jyotsana Pathak ◽  
Kamla Rawat ◽  
V. K. Aswal ◽  
H. B. Bohidar
Keyword(s):  
Aqueous Solution ◽  
Protein Separation ◽  
Globular Proteins ◽  
Representative Model

Representative model of protein–protein separation in a BSA–GB–β-Lg aqueous solution.

Static structure factor and collective diffusion of globular proteins in concentrated aqueous solution

1996 ◽  
Vol 104 (1) ◽  
pp. 326-335 ◽  
Author(s):  
Bernard M. Fine ◽  
Aleksey Lomakin ◽  
Olutayo O. Ogun ◽  
George B. Benedek
Keyword(s):  
Aqueous Solution ◽  
Structure Factor ◽  
Globular Proteins ◽  
Static Structure Factor ◽  
Static Structure

Interaction of n-octyl-β-d-glucopyranoside with globular proteins in aqueous solution

1988 ◽  
Vol 10 (5) ◽  
pp. 270-276 ◽  
Author(s):  
Julia Cordoba ◽  
Miguel D. Reboiras ◽  
Malcolm N. Jones
Keyword(s):  
Aqueous Solution ◽  
Globular Proteins

Effect of Zein Concentration on the Formation of Pectin-Zein Complexes

2012 ◽  
Vol 506 ◽  
pp. 319-322 ◽  
Author(s):  
Maneerat Juttulapa ◽  
Pornsak Sriamornsak
Keyword(s):  
Aqueous Solution ◽  
Zeta Potential ◽  
Physicochemical Properties ◽  
Isoelectric Point ◽  
Globular Proteins ◽  
Ph Values ◽  
Anionic Polysaccharides ◽  
Formation Of Complexes

Biopolymeric particles can be formed by electrostatic complexes of globular proteins and anionic polysaccharides mixtures at pH values above pKa of anionic polysaccharide and under the isoelectric point of protein. The purpose of this study was to investigate the effect of protein (i.e., zein) concentration on the formation of complexes between zein and polysaccharide (i.e., amidated low methoxy pectin) in aqueous solution. The zeta potential, turbidity and morphology under different conditions were observed to provide insights into the physicochemical properties of zein-pectin complexes. The biopolymeric particles were obtained at pH 4 and concentration of zein and pectin of 0.001 and 1% w/w, respectively. As the zein concentration increased, the turbidity of zein-pectin solutions increased, resulting from the formation of zein-pectin complexes. The zeta potential of the systems became less negative when the zein concentration increased. The results suggested that concentration of zein primarily influenced the formation of zein-pectin complexes.

The Enthalpy of Interaction of Urea with Some Globular Proteins

1976 ◽  
Vol 66 (1) ◽  
pp. 127-131 ◽  
Author(s):  
Maria I. PAZ ANDRADE ◽  
Malcolm N. JONES ◽  
Henry A. SKINNER
Keyword(s):  
Globular Proteins ◽  
Enthalpy Of Interaction
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