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Biophysical chemistry is a physical science that uses the concepts of physics and physical chemistry for the study of biological systems. [1] The most common feature of the research in this subject is to seek an explanation of the various phenomena in biological systems in terms of either the molecules that make up the system or the supra-molecular structure of these systems. [2]
Physical biochemistry is a branch of biochemistry that deals with the theory, techniques, and methodology used to study the physical chemistry of biomolecules. [1] It also deals with the mathematical approaches for the analysis of biochemical reaction and the modelling of biological systems. It provides insight into the structure of ...
The Journal of Proteomics is a peer-reviewed scientific journal published by Elsevier. It is the official journal of the European Proteomics Association and the editor-in-chief is Juan Calvete. [1] It was established in 1979 as the Journal of Biochemical and Biophysical Methods, [2] obtaining its current name in 2008. [3]
S. Scatchard equation; Schild equation; Searching the conformational space for docking; Sedimentation equilibrium; Sephadex; Sequencing; Shotgun lipidomics
In these methods, a reacting system initially at equilibrium is perturbed rapidly and then observed as it relaxes back to equilibrium. [ 1 ] [ 2 ] [ 3 ] In the case of temperature jump, the perturbation involves rapid heating which changes the value of the equilibrium constant , followed by relaxation to equilibrium at the new temperature.
Loop-mediated isothermal amplification (LAMP) primers [1] Loop-mediated isothermal amplification (LAMP) product [1]. In LAMP, the target sequence is amplified at a constant temperature of 60–65 °C (140–149 °F) using either two or three sets of primers and a polymerase like Bst Klenow fragment with high strand displacement activity in addition to a replication activity.
The most common method of measuring amino acid hydrophobicity is partitioning between two immiscible liquid phases. Different organic solvents are most widely used to mimic the protein interior. However, organic solvents are slightly miscible with water and the characteristics of both phases change making it difficult to obtain pure ...
This reaction is rapid and stoichiometric, with the addition of one mole of thiol releasing one mole of TNB. The TNB 2− is quantified in a spectrophotometer by measuring the absorbance of visible light at 412 nm, using an extinction coefficient of 14,150 M −1 cm −1 for dilute buffer solutions, [4] [5] and a coefficient of 13,700 M −1 cm −1 for high salt concentrations, such as 6 M ...