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Detection of Prion Protein Intermolecular Interaction by Electrophoresis and Western Blot
Author(s) -
Ayman S. Moussa
Publication year - 2015
Publication title -
journal of chromatography and separation techniques
Language(s) - English
Resource type - Journals
ISSN - 2157-7064
DOI - 10.4172/2157-7064.1000e131
Subject(s) - western blot , prion protein , intermolecular force , protein detection , electrophoresis , intermolecular interaction , chemistry , computational biology , biology , biochemistry , nanotechnology , materials science , gene , medicine , molecule , disease , organic chemistry , pathology
Copyright: © 2015 Moussa A. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. In biochemistry and pharmacology, a ligand is generally a small molecule that forms a complex with a biomolecule to serve a biological purpose. The binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and van der Waals forces. In general, highaffinity binding involves a longer residence time for the ligand at its receptor binding site than is the case for low-affinity binding. Highaffinity binding of ligands is often physiologically important as some of the binding energy can be used to cause a conformational change. The hydrogen bond is often described as a strong electrostatic dipole-dipole interaction, has some covalent bonding features, usually involves a limited number of interaction partners and produces interatomic distances shorter than the sum of van der Waals radius.

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