title: Comparison between UV Raman and circular dichroism detection of short alpha helices in bombolitin III.
abstract: We have used UV resonance Raman (UVRR) and circular dichroism (CD) spectroscopies to examine the dilute solution-phase secondary structure of the 17 amino acid peptide Bombolitin III (BIII). Both UVRR and CD clearly observe the alpha-helix structure induced by the addition of trifluoroethanol (TFE) to BIII. In contrast, only UVRR is able to detect the single alpha-helical turn induced by increasing the pH of BIII from pH 1.8 to 6.4. This alpha-helical turn is formed because of a stabilizing salt bridge formed between Lys(2) and Asp(5). Further increases in the alpha-helix content occur as the pH is raised further. We compare the relative sensitivity of UVRR and CD to short alpha helices and find, as expected, that the CD cannot detect short alpha helices. This study demonstrates that UV Raman measurements can detect the formation of single alpha-helical turns which cannot be detected by CD measurements.
authors.affiliation: Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260.
authors.forename: Abdil
authors.initials: A
authors.lastname: Ozdemir
authors.forename: Igor K
authors.initials: IK
authors.lastname: Lednev
authors.forename: Sanford A
authors.initials: SA
authors.lastname: Asher
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman
chemical_list: D010455:Peptides; C044299:bombolitins