Title
Protein Analysis By Dynamic Light Scattering: Methods And Techniques For Students
Keywords
Light scattering; Protein; Temperature; Viscosity
Abstract
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. 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. It reviews the basic concepts of light scattering measurements and addresses four critical aspects of the analysis and interpretation of DLS results. 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. Variables like temperature, solvent viscosity, and inter-particle interactions may also influence particle size determination. 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. © 2012 Wiley Periodicals, Inc.
Publication Date
11-1-2012
Publication Title
Biochemistry and Molecular Biology Education
Volume
40
Issue
6
Number of Pages
372-382
Document Type
Article
Personal Identifier
scopus
DOI Link
https://doi.org/10.1002/bmb.20644
Copyright Status
Unknown
Socpus ID
84869789038 (Scopus)
Source API URL
https://api.elsevier.com/content/abstract/scopus_id/84869789038
STARS Citation
Lorber, Bernard; Fischer, Frédéric; Bailly, Marc; Roy, Hervé; and Kern, Daniel, "Protein Analysis By Dynamic Light Scattering: Methods And Techniques For Students" (2012). Scopus Export 2010-2014. 4738.
https://stars.library.ucf.edu/scopus2010/4738