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Biophys Rev. 2016 Dec;8(4):409-427. doi: 10.1007/s12551-016-0218-6. Epub 2016 Oct 6.

Dynamic light scattering: a practical guide and applications in biomedical sciences.

Author information

1
Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, R3T 2N2, Canada. jorg.stetefeld@ad.umanitoba.ca.
2
Department of Biochemistry and Medical Genetics, University of Manitoba, 745 Bannatyne Avenue - Basic Medical Sciences Building, Winnipeg, Manitoba, R3E 0J9, Canada. jorg.stetefeld@ad.umanitoba.ca.
3
Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, R3T 2N2, Canada.
4
Department of Biochemistry and Medical Genetics, University of Manitoba, 745 Bannatyne Avenue - Basic Medical Sciences Building, Winnipeg, Manitoba, R3E 0J9, Canada.
5
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. trushar.patel@uleth.ca.
6
Alberta RNA Research and Training Institute, Department of Chemistry & Biochemistry, University of Lethbridge, 4401 University Drive, Lethbridge, Alberta, T1K 3M4, Canada. trushar.patel@uleth.ca.

Abstract

Dynamic light scattering (DLS), also known as photon correlation spectroscopy (PCS), is a very powerful tool for studying the diffusion behaviour of macromolecules in solution. The diffusion coefficient, and hence the hydrodynamic radii calculated from it, depends on the size and shape of macromolecules. In this review, we provide evidence of the usefulness of DLS to study the homogeneity of proteins, nucleic acids, and complexes of protein-protein or protein-nucleic acid preparations, as well as to study protein-small molecule interactions. Further, we provide examples of DLS's application both as a complementary method to analytical ultracentrifugation studies and as a screening tool to validate solution scattering models using determined hydrodynamic radii.

KEYWORDS:

Analytical ultracentrifuge; Diffusion coefficient; Dynamic light scattering; Hydrodynamic radius; Light scattering; Protein–ligand interactions; Protein–nucleic acid complexes; Protein–protein complexes

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