Encyclopedia of Biophysics

2013 Edition
| Editors: Gordon C. K. Roberts

Far UV Protein Circular Dichroism

Reference work entry
DOI: https://doi.org/10.1007/978-3-642-16712-6_634

Synonyms

Definition

Protein circular dichroism (CD) spectroscopy is usually divided into (1) far UV or backbone (meaning the amide transitions, Fig.  1) with data collected from ~190 to 250 nm and (2) near UV or aromatic with data collected from 250 to 300 nm. The practical reason for the division is that the absorbance magnitudes of the two regions for a typical protein differ by ~2 orders of magnitude. In addition, the far UV CD spectrum of a protein contains information about the asymmetric features of the backbone of proteins whereas the near UV depends on the orientations and environments of the side chains. The challenge is to extract the structural information. The most common reason for collecting protein CD data is to assign secondary structure content by expressing the spectra as a combination of standard spectra which are then deconvoluted to give the percentages of a limited number of well-defined...
This is a preview of subscription content, log in to check access.

References

  1. Anderluh G, Gökçe I, Lakey JH. A natively unfolded toxin domain uses its receptor as a folding template. J Biol Chem. 2004;279:22002–9.PubMedGoogle Scholar
  2. Berova N, Woody RW, Polavarapu P, Nakanishi K. Comprehensive chiroptical spectroscopy (in press).Google Scholar
  3. Cooper TM, Woody RW. The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosin. Biopolymers. 1990;30:657–76.PubMedGoogle Scholar
  4. Gokce I, Woody RW, Anderluh G, Lakey JH. Single peptide bonds exhibit poly(pro)II (“random coil”) circular dichroism spectra. J Am Chem Soc. 2005;127:9700–1.PubMedGoogle Scholar
  5. Johnson WC. Analyzing protein circular dichroism spectra for accurate secondary structures. Protein Struct Funct Genet. 1999;35:307–12.Google Scholar
  6. Miguel MS, Marrington R, Rodger PM, Rodger A, Robinson C. An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on hydrophobicity of the environment. Eur J Biochem. 2003;270:3345–52.Google Scholar
  7. Nordén B, Rodger A, Dafforn TR. Linear dichroism and circular dichroism: a textbook on polarized spectroscopy. Cambridge: Royal Society of Chemistry; 2010.Google Scholar
  8. Rodger A, Nordén B. Circular dichroism and linear dichroism. Oxford: Oxford University Press; 1997.Google Scholar
  9. Wallace BA, Janes R, editors. Modern techniques for circular dichroism spectroscopy. Amsterdam: IOS Press; 2009.Google Scholar

Copyright information

© European Biophysical Societies' Association (EBSA) 2013

Authors and Affiliations

  1. 1.Department of ChemistryUniversity of WarwickCoventryUK