Journal ArticleDOI
Hydrophobic (interaction) chromatography.
About:
This article is published in Biochimie.The article was published on 1978-03-31. It has received 89 citations till now. The article focuses on the topics: Hydrophilic interaction chromatography & Reversed-phase chromatography.read more
Citations
More filters
Journal ArticleDOI
Hydrophobic interaction chromatography of proteins.
TL;DR: The different proposed theories for the retention mechanism of proteins in HIC are presented and the main parameters to consider for the optimization of fractionation processes by HIC and the stationary phases available were described.
Journal ArticleDOI
Purification and characterization of toxins A and B of Clostridium difficile.
TL;DR: The initial step of the purification scheme involved ultrafiltration through an XM-100 membrane filter and ion-exchange chromatography on DEAE-NaCl gradients, which failed to increase the specific activity of toxin B, but provided additional evidence that the two toxins are distinct molecules.
Book ChapterDOI
Hydrophobic interactions: role in bacterial adhesion
Mel Rosenberg,Staffan Kjelleberg +1 more
TL;DR: The aims of the present chapter are to present some relevant aspects of hydrophobic interactions, describe the methodology available for measurements related to bacterial cell-surface hydrophobicity and the parameters they may measure, and discuss investigations dealing with surface components that promote or reduce bacterial hydrophobia.
Journal ArticleDOI
Hydrophobic charge induction chromatography: salt independent protein adsorption and facile elution with aqueous buffers
TL;DR: A new form of protein chromatography, hydrophobic charge induction, is described, which could be carried out within the pH 5-9 range and matched to protein requirements by ligand choice and density.
Journal ArticleDOI
Peptide adsorption on silica nanoparticles: evidence of hydrophobic interactions
Valeria Puddu,Carole C. Perry +1 more
TL;DR: The studies show how it is possible to modulate peptide uptake on silica, or in fact on any particle, by changing either the surface properties or the binding environment, and suggest a multistep adsorption mechanism leading to the formation of multilayers onsilica.
References
More filters
Journal ArticleDOI
The interpretation of protein structures: estimation of static accessibility.
B. Lee,Frederic M. Richards +1 more
TL;DR: The accessibility of atoms in the twenty common amino acids in model tripeptides of the type Ala-X-Ala are given for defined conformation and the larger non-polar amino acids tend to be more “buried” in the native form of all three proteins.
Book ChapterDOI
Some factors in the interpretation of protein denaturation.
TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
Book
The Hydrophobic Effect: Formation of Micelles and Biological Membranes
TL;DR: In this article, the authors discuss the properties of water molecules and their relationship with common soluble proteins, such as membrane proteins and membrane membrane proteins, as well as the effect of temperature on their properties.
Journal ArticleDOI
Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads.
TL;DR: It is demonstrated that successful application of affinity chromatography in many cases will critically depend on placing the ligand at a considerable distance from the matrix backbone.
Journal ArticleDOI
Free Volume and Entropy in Condensed Systems III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes
Henry S. Frank,Marjorie W. Evans +1 more
TL;DR: The first and second papers in this series, which make it possible to interpret entropy data in terms of a physical picture, are applied to binary solutions, and equations are derived relating energy and volume changes when a solution is formed to the entropy change for the process as discussed by the authors.