PROTEIN-STRUCTURE AND STABILITY ASSESSMENT BY CIRCULAR-DICHROISM SPECTROSCOPY

With the advent of biotechnology and recombinant DNA methodology, there has been a renewed interest in protein folding and protein stability. One of the most powerful techniques available for the study of changes in protein structure is circular dichroism (CD) spectroscopy. Various applications of CD spectroscopy to the study of proteins are described, including analysis of denaturation curves, calculation of secondary structure composition, observation of changes in both secondary and tetriary structure, characterization of folding intermediates, and evaluation of the effects of site-directed mutagenesis. Finally, a case study on fibrolase, a metalloprotease from snake venom, is presented.