Stabilization of proteins by solvents. Effect of pH and anions on the positive cooperativity of 2-nonanone binding to bovine serum albumin.
S Damodaran,J E Kinsella +1 more
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The binding of 2-nonanone to bovine serum albumin exhibited positive cooperativity at low molal ratios of binding, indicating stabilization of the hydrophobic binding sites at low concentrations of 2 nonanone, and the degree of cooperativity was affected by the type of anion present.About:
This article is published in Journal of Biological Chemistry.The article was published on 1980-09-25 and is currently open access. It has received 24 citations till now. The article focuses on the topics: Cooperativity & Bovine serum albumin.read more
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The Hofmeister effect and the behaviour of water at interfaces.
TL;DR: The first general, detailed qualitative molecular mechanism for the origins of ion-specific (Hofmeister) effects on the surface potential difference at an air-water interface is proposed; this mechanism suggests a simple model for the behaviour of water at all interfaces, regardless of whether the non-aqueous component is neutral or charged, polar or non-polar.
Book ChapterDOI
Physicochemical and functional properties of oilseed proteins with emphasis on soy proteins
Journal ArticleDOI
Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry.
TL;DR: The three melting transitions are consistent in origin with the cooperative unfolding of three unique immunoglobulin-like domains of IL-1R with a correlation between the predicted ranking of stability and the extent of aggregation demonstrated using DSC.
Journal ArticleDOI
Proteomics and models for enzyme cooperativity.
TL;DR: The type of cooperativity that will be the focus of this review is “allosteric cooperativity”, which has been used to describe a ligand-enzyme interaction, which results in a measurable conformational change in proximal and distal regions of that protein.
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Interactions of Milk Proteins and Volatile Flavor Compounds: Implications in the Development of Protein Foods
TL;DR: In this paper, the binding of volatile flavor compounds by milk proteins in aqueous solutions is discussed and compared in terms of their binding affinity for flavor compounds, and the influence of temperature and ultra-high pressures on the interactions between proteins and flavors is considered in detail.
References
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The Attractions of Proteins for Small Molecules and Ions
TL;DR: The number and variety of known compounrjs between proteins and small molecules are increasing rapidly and make a fascinating story as discussed by the authors, and there are many compounds of serum albumin, which was used during the war by many chemists, most of whom found at least one 6ew compound.
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On the Nature of Allosteric Transitions: A Plausible Model
TL;DR: "It is certain that all bodies whatsoever, though they have no sense, yet they have perception, and whether the body be alterant or alterec, evermore a perception precedeth operation; for else all bodies would be like one to another."
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.
Journal ArticleDOI
A relation between non-esterified fatty acids in plasma and the metabolism of glucose
Journal ArticleDOI
Zur Lehre von der Wirkung der Salze
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The effects of neutral salts on the stability of macromolecules. A new approach using a protein-ligand binding system.
S Damodaran,J E Kinsella +1 more