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
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Status: |
Published |
Creators/Authors: |
Creators | Email | Pitt Username | ORCID  |
---|
Ozdemir, A | | | | Lednev, IK | | | | Asher, SA | asher@pitt.edu | ASHER | |
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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: |
22 Jun 2021 13:55 |
URI: |
http://d-scholarship.pitt.edu/id/eprint/17797 |
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