Curious to learn how light scattering provides label-free, immobilization-free, first-principles characterization of macromolecular interactions? Download this open-access publication!
Protein Interactions, J. Cai and R.E. Wang (Ed.), InTech, 2012
By Daniel Some and Sophia Kenrick
Macromolecular interactions play key roles in a host of scientific and biotechnological studies—from basic biomolecular research to protein therapeutic R&D. Light scattering measurements quantify these phenomena without tagging, immobilization, or other sample modifications that can potentially skew the interaction of interest. Composition Gradient Multi-Angle static Light Scattering (CG-MALS) and Composition-Gradient Dynamic Light Scattering (CG-DLS) determine a variety of quantitative interaction parameters, including equilibrium dissociation constants (KD), stoichiometry, virial coefficients (A2) and reaction rates. Recent advances in instrumentation and technique simplify and automate measurements, resulting in hands-off operation with excellent repeatability.
The first half of the chapter reviews the theory and practice of CG-MALS and CG-DLS. The second half focuses on a range of applications, including:
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Protein self-association as a function of ionic strength, pH, and other excipients
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Hetero-association between two proteins with various stoichiometries
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Self-assembly of multivalent protein complexes
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Dissociation kinetics
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Nonspecific attractive and repulsive interactions
Figure 1: Quantification of self (a) and hetero-associations (b-c) by composition-gradient multi-angle light scattering (CG-MALS)
Location of book image: http://www.intechopen.com/books/protein-interactions
