title: Structural analysis of unfolded peptides by Raman spectroscopy.
abstract: Raman spectroscopy has positioned itself as an invaluable tool in the study of complex biological systems, consistently being used to obtain information illustrating a vast array of fundamental properties. Of primary interest, with respect to the focus of this chapter, are conformational changes of peptide backbones. For short peptides to larger biological systems this understanding can be extended to local hydrogen bonding interactions and the probing of other structural or organizational properties. With regard to unfolded peptides Raman spectroscopy can be used as a technique complementary to infrared (IR) and vibrational circular dichroism (VCD) spectroscopy. This chapter describes how high quality polarized Raman spectra of peptide can be recorded with a Raman microspectrometer and how the structure sensitive amide I band profiles of isotropic and anisotropic Raman scattering can be analyzed in conjunction with the respective IR and VCD profiles to obtain conformational distributions of short unfolded peptides.
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: Siobhan
authors: S
authors: Toal
authors: Daniel
authors: D
authors: Verbaro
mesh_terms: D000465:Algorithms; D016880:Anisotropy; D002138:Calibration; D003627:Data Interpretation, Statistical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D058767:Protein Unfolding; D012015:Reference Standards; D012984:Software; D013059:Spectrum Analysis, Raman / Q000592:standards
chemical_list: D010455:Peptides