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Comparison between UV Raman and circular dichroism detection of short α helices in bombolitin III

Ozdemir, A and Lednev, IK and Asher, SA (2002) Comparison between UV Raman and circular dichroism detection of short α helices in bombolitin III. Biochemistry, 41 (6). 1893 - 1896. ISSN 0006-2960

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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 α-helix structure induced by the addition of trifluoroethanol (TFE) to BIII. In contrast, only UVRR is able to detect the single α-helical turn induced by increasing the pH of BIII from pH 1.8 to 6.4. This α-helical turn is formed because of a stabilizing salt bridge formed between Lys2 and Asp5. Further increases in the α-helix content occur as the pH is raised further. We compare the relative sensitivity of UVRR and CD to short α helices and find, as expected, that the CD cannot detect short α helices. This study demonstrates that UV Raman measurements can detect the formation of single α-helical turns which cannot be detected by CD measurements.

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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Ozdemir, A
Lednev, IK
Asher, SAasher@pitt.eduASHER
Date: 12 February 2002
Date Type: Publication
Journal or Publication Title: Biochemistry
Volume: 41
Number: 6
Page Range: 1893 - 1896
DOI or Unique Handle: 10.1021/bi010970e
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 0006-2960
MeSH Headings: Amino Acid Sequence; Circular Dichroism; Molecular Sequence Data; Peptides--chemistry; Protein Structure, Secondary; Spectrum Analysis, Raman
PubMed ID: 11827535
Date Deposited: 20 Mar 2013 16:43
Last Modified: 12 Jun 2021 23:55
URI: http://d-scholarship-dev.library.pitt.edu/id/eprint/17797

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