Foaming behavior of sugar-based surfactants: influence of molecular structure and anticipation from surface properties

Author(s):  
Rémy Bois ◽  
Isabelle Pezron ◽  
Patricia Rotureau ◽  
Elisabeth Van Hecke ◽  
Guillaume Fayet ◽  
...  
2015 ◽  
Vol 132 ◽  
pp. 45-53 ◽  
Author(s):  
M. Jarpa-Parra ◽  
F. Bamdad ◽  
Z. Tian ◽  
Hongbo Zeng ◽  
Feral Temelli ◽  
...  

2010 ◽  
Vol 43 (24) ◽  
pp. 10481-10489 ◽  
Author(s):  
Jae-Seung Chung ◽  
Byoung Gak Kim ◽  
Eun-Ho Sohn ◽  
Jong-Chan Lee

Soft Matter ◽  
2020 ◽  
Vol 16 (30) ◽  
pp. 7063-7076
Author(s):  
Polina Naidjonoka ◽  
Monica Arcos Hernandez ◽  
Gunnar K. Pálsson ◽  
Frank Heinrich ◽  
Henrik Stålbrand ◽  
...  

The relation between bulk and surface properties of hemicelluloses is investigated in order to shed light on the hemicellulose/cellulose interactions.


2021 ◽  
Vol 28 ◽  
Author(s):  
Sen Tang ◽  
Junsheng Li ◽  
Guoxia Huang ◽  
Liujuan Yan

: This article reviews and discusses the relationship between surface hydrophobicity and other surface properties of proteins and the possibility of using surface hydrophobicity as a key indicator to predict and evaluate the changes in the surface properties of a protein. Hydrophobicity is the main driving force of protein folding; it affects the structure and functions. Surface hydrophobicity and other surface properties of proteins are controlled by their spatial structures. Due to the hydrophobic interactions, most proteins fold into their globular structures, and they lack sufficient hydrophobic residues on the molecular surface; thus, they do not exhibit excellent surface properties. Surface hydrophobicity is closely related to the changes in the surface property of proteins because it directly reflects the actual distribution of the hydrophobic residues on the surface of a protein. The molecular structure of a protein can be changed or modified to remove the constraints of spatial structures and expose more hydrophobic residues on the molecular surface, which may improve the surface properties of proteins. Therefore, the changes in the surface hydrophobicity caused by changes in the molecular structure can be an ideal key indicator to predict and evaluate the changes in the surface properties of a protein.


1996 ◽  
Vol 179 (2) ◽  
pp. 327-334 ◽  
Author(s):  
Remco Tuinier ◽  
Chris G.J. Bisperink ◽  
Cor van den Berg ◽  
Albert Prins

Author(s):  
D.C. Hixson ◽  
J.C. Chan ◽  
J.M. Bowen ◽  
E.F. Walborg

Several years ago Karasaki (1) reported the production of type C virus particles by Novikoff ascites hepatocarcinoma cells. More recently, Weinstein (2) has reported the presence of type C virus particles in cell cultures derived from transplantable and primary hepatocellular carcinomas. To date, the biological function of these virus and their significance in chemically induced hepatocarcinogenesis are unknown. The present studies were initiated to determine a possible role for type C virus particles in chemically induced hepatocarcinogenesis. This communication describes results of studies on the biological and surface properties of type C virus associated with Novikoff hepatocarcinoma cells.Ecotropic and xenotropic murine leukemia virus (MuLV) activity in ascitic fluid of Novikoff tumor-bearing rats was assayed in murine sarcoma virus transformed S+L- mouse cells and S+L- mink cells, respectively. The presence of sarcoma virus activity was assayed in non-virus-producing normal rat kidney (NRK) cells. Ferritin conjugates of concanavalin A (Fer-Con wheat germ agglutinin (Fer-WGA), and Ricinus communis agglutinins I and II (Fer-RCAI and Fer-RCAII) were used to probe the structure and topography of saccharide determinants present on the viral envelope.


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