Application of circular dichroism spectroscopy in studying protein folding, stability, and interaction

Md Anzarul Haque, Punit Kaur, Asimul Islam, Md Imtaiyaz Hassan

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

Abstract

Circular dichroism (CD) is a powerful spectroscopic technique used to study the changes in the structure and conformation of a protein. The wavelength ranges used for the structural assessment of protein are broadly classified into three regions. Far-UV CD (190-250 nm) is used to measure the secondary structure of proteins, which monitors any change in the peptide backbone. The near-UV CD (250-320 nm) monitors changes in the vicinity of aromatic amino acids in a protein, investigating the tertiary structure of proteins. Visible CD (350-700 nm) is used for monitoring the interaction of prosthetic groups (various metal ions) with proteins. Strong extrinsic CD bands of the extrinsic chromophore and intrinsic CD signals of protein can also be used to monitor protein-ligand interaction. Characteristic bands of aromatic residues (Trp, Tyr, and Phe) in the near-UV region can be used to examine the effect of mutations on the tertiary structure of proteins. This chapter presents an in-depth overview of CD spectroscopy’s basic principles, technical details, and applications.

Original languageEnglish (US)
Title of host publicationAdvances in Protein Molecular and Structural Biology Methods
PublisherElsevier
Pages213-224
Number of pages12
ISBN (Electronic)9780323902649
ISBN (Print)9780323902656
DOIs
StatePublished - Jan 1 2022
Externally publishedYes

Keywords

  • CD spectroscopy
  • Optical rotation
  • Protein folding
  • Structural dynamics

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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