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Theory and Practice of CG-MALS Book Chapter

 

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:
 
  • Protein self-association as a function of ionic strength, pH, and other excipients

  • Hetero-association between two proteins with various stoichiometries

  • Self-assembly of multivalent protein complexes

  • Dissociation kinetics

  • 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