Book chapter
Structural Analysis of Unfolded Peptides by Raman Spectroscopy
Intrinsically Disordered Protein Analysis, pp 315-346
31 May 2012
PMID: 22760326
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.
Metrics
15 Record Views
7 citations in Scopus
Details
- Title
- Structural Analysis of Unfolded Peptides by Raman Spectroscopy
- Creators
- Reinhard Schweitzer-Stenner - Department of Chemistry, Drexel University, Philadelphia, USAJonathan B Soffer - Department of Chemistry, Drexel University, Philadelphia, USASiobhan Toal - Department of Chemistry, Drexel University, Philadelphia, USADaniel Verbaro - Department of Chemistry, Drexel University, Philadelphia, USA
- Publication Details
- Intrinsically Disordered Protein Analysis, pp 315-346
- Series
- Methods in Molecular Biology
- Publisher
- Humana Press; Totowa, NJ
- Resource Type
- Book chapter
- Language
- English
- Academic Unit
- Chemistry
- Scopus ID
- 2-s2.0-84865342686
- Other Identifier
- 991014877973604721