Abstract

Publisher Summary Experimental observations in recent years that the mechanism by which a protein is converted to amyloid is related intimately to conformational changes have caused an increased interest in the various methodologies for analyzing protein conformation and structure. Thus, research associated with amyloid diseases has truly become an interdisciplinary field, involving scientists from areas as diverse as clinical medicine and biophysical chemistry. The increasing volume of literature on biophysical studies of amyloidogenic peptides and proteins has made it necessary for amyloid researchers to have a basic understanding of, and perhaps apply, some of the common spectroscopic methods available to gain structural information on amyloidogenic proteins. This chapter provides a practical guide to amyloid researchers on the most commonly used spectroscopic techniques to study protein structure, which are ultraviolet visible (UV/Vis) fluorescence, and circular dichroism (CD) spectroscopy. The spectroscopic techniques discussed in this chapter can provide complementary information on the structure of proteins. The technique of choice depends on many factors, including instrument availability, protein concentration needed, solvent conditions, protein availability, and the structural information desired.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.