title: Structure analysis of unfolded peptides I: vibrational circular dichroism spectroscopy.
abstract: Vibrational circular dichroism (VCD) spectroscopy is an invaluable spectroscopic techniques utilized to exploit the optical strength of vibrational transitions for structure analysis. In this chapter, we describe the protocol for measuring and self-consistently analyzing VCD and the corresponding FT-IR spectra of short peptides. This process involves the decomposition of the IR spectrum as well as simulations of the amide I band profiles in both spectra based on structural models of the peptides investigated. This type of spectral analysis should be complemented with similar investigations of Raman spectra, which are described in the subsequent chapter. The structural analysis of short, unfolded peptides described in this chapter can easily be extended for the analysis of longer unfolded peptides or even proteins. This is particularly important in view of the demonstrated biological relevance of intrinsically disordered peptides and proteins (IDPs).
authors: Department of Chemistry, Drexel University, Philadelphia, PA, USA. rschweitzer-stenner@drexel.edu
authors: Reinhard
authors: R
authors: Schweitzer-Stenner
authors: Jonathan B
authors: JB
authors: Soffer
authors: Daniel
authors: D
authors: Verbaro
mesh_terms: D000465:Algorithms; D002942:Circular Dichroism; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012984:Software; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D010455:Peptides