Binding of globular proteins to DNA from surface tension measurement.
نویسندگان
چکیده
Extent of binding (gammap) of globular proteins to calf-thymus DNA have been measured in mole per mole of nucleotide as function of equilibrium protein concentration. We have exploited measurement of the surface tension of the protein solution in the presence and absence of DNA to calculate the binding ration (gammap). Interaction of bovine serum albumin with DNA has been studied at different pH. Interaction of bovine serum albumin with DNA has been studied at different pH, ionic strength and in presence of Ca2+. Interaction of BSA with denatured DNA has also been investigated. Binding isotherms for other globular proteins like beta-lactoglobulin, alpha-lactalbumin and lysozyme have been compared under identical physicochemical condition. It has been noted with considerable interest that globular form of protein is important to some extent in protein-DNA interaction. An attempt has been made to explain the significance of difference in binding ratios of these two biopolymers in aqueous medium for different systems in the light of electrostatic and hydrophobic effects. Values of maximum binding ration (gammap(m)) at saturated level for different systems have been also presented. The Gibb's free energy decrease (-deltaG0) of the binding of proteins to DNA has been compared more precisely for the saturation of binding sites in the DNA with the change of activity of protein in solution from zero to unity in the rational mole fraction scale.
منابع مشابه
Rapid purification of HU protein from Halobacillus karajensis
The histone-like protein HU is the most-abundant DNA-binding protein in bacteria. The HU protein non-specifically binds and bends DNA as a hetero- or homodimer, and can participate in DNA supercoiling and DNA condensation. It also takes part in DNA functions such as replication, recombination, and repair. HU does not recognize any specific sequences but shows a certain degree of specificity to ...
متن کاملThe Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) Genes among Clinical Isolates of Staphylococcus aureus from Hospitalized Children
Background:Isolates of Staphylococcus aureus express a myriad of adhesive surface proteins that play important role in colonization of the bacteria on nasal and skin surfaces, beginning the process of pathogenesis. The aim of this study was to screen several of the Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) genes among the isolate of S. a...
متن کاملSTU DIES ON THE BINDING OF THE ALKYLATING AGENT SULFUR MUSTARD TO CALF THYMUS CHROMATIN
In this study the effect of the alkylating agent, sulfur mustard, on calf thymus chromatin was investigated using UV/Vis spectroscopy, gel electrophoresis and thermal denaturation techniques. The results show that treatment of isolated chromatin with sulfur mustard releases histones from the core particles but does not affect histone H I and nonhistone chromosomal proteins. The content of ...
متن کاملLow-density/high-density liquid phase transition for model globular proteins.
The effect of molecule size (excluded volume) and the range of interaction on the surface tension, phase diagram, and nucleation properties of a model globular protein is investigated using a combination of Monte Carlo simulations and finite temperature classical density functional theory calculations. We use a parametrized potential that can vary smoothly from the standard Lennard-Jones intera...
متن کاملProduction of Electrospun Nanofibers from Food Proteins and Polysaccharides and Their Applications in Food and Drug Sciences
Preparation of nano-microfibers from biopolymers (e.g., proteins and polysaccharides) by using electrospinning technology has been considered by researchers due to the formation of fibers or particles at the nano and micrometer scales, high porosity level, adjustable dewatering behavior, and special mechanical behavior. These products can be used in the microencapsulation of bioactive compounds...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Indian journal of biochemistry & biophysics
دوره 38 5 شماره
صفحات -
تاریخ انتشار 2001