![]() ![]() For half a century they have been used to monitor aggregation phenomena in protein solutions. Light scattering measurements have numerous applications in condensed matter physics, biology, and medicine. Amongst them, noninvasive spectroscopic methods based on light scattering have become a popular tool in biomolecule characterization. An increasing number of instruments based on physical methods have appeared in biology laboratories. © 2012 by The International Union of Biochemistry and Molecular Biologyĭuring the last two decades the panel of methods used to study the structure and function of proteins and nucleic acids has grown continuously. Every point is illustrated by case studies, including a commercially available albumin, a small RNA virus isolated from plants, as well as four soluble proteins and a ribonucleoprotein assembly purified and characterized by students in the frame of their master degree. Variables like temperature, solvent viscosity, and inter-particle interactions may also influence particle size determination. To ensure reproducible quantitative data, attention should be paid to controlling the preparation and handling of proteins or assemblies because variations in the state of aggregation, induced by minor changes in experimental condition or technique, might compromise DLS results and affect protein activity. It reviews the basic concepts of light scattering measurements and addresses four critical aspects of the analysis and interpretation of DLS results. ![]() This article is written for graduate and undergraduate students with access to DLS and for faculty members who wish to incorporate DLS into a lab activity, a practical course or research. Dynamic light scattering (DLS) analyses are routinely used in biology laboratories to detect aggregates in macromolecular solutions, to determine the size of proteins, nucleic acids, and complexes or to monitor the binding of ligands. ![]()
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