Journal article
Salmon calcitonin and amyloid beta: two peptides with amyloidogenic capacity adopt different conformational manifolds in their unfolded states
Biochemistry (Easton), v 45(9), pp 2810-2819
07 Mar 2006
PMID: 16503636
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The molecular conformations of salmon calcitonin in aqueous solution have been investigated by exploiting the different influences of excitonic coupling on the amide I band profile in the isotropic and anisotropic Raman, FTIR, and vibrational circular dichroism spectra of a polypeptide. The N-terminal loop, caused by a disulfide bridge between cysteines at positions 1 and 7, was modeled by performing a conformational search by molecular mechanics calculations. The remaining part of the peptide chain was modeled as a mixture of three sequences containing different fractions of residues adopting poly-l-proline II (PPII), extended beta-strand, and alpha-helix-like conformations. This yielded an excellent reproduction of the experimentally observed amide I' band profiles. A comparison with recent data on the beta-amyloid fragment Abeta(1)(-)(28) revealed a lower PPII content and more conformational heterogeneity for calcitonin. Thus, our results underscore the notion that individual structural propensities of amino acid residues give rise to structural differences between the unfolded states of even long peptide chains, at variance with expectations based on a random or statistical coil model.
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Details
- Title
- Salmon calcitonin and amyloid beta: two peptides with amyloidogenic capacity adopt different conformational manifolds in their unfolded states
- Creators
- Reinhard Schweitzer-Stenner - Department of Chemistry, Drexel University, 32nd and Chestnut Streets, Philadelphia, Pennsylvania 19104, USA. rschweitzer-stenner@drexel.eduThomas MeaseyAndrew HagarmanFatma EkerKai Griebenow
- Publication Details
- Biochemistry (Easton), v 45(9), pp 2810-2819
- Publisher
- American Chemical Society; Washington, DC
- Grant note
- P20 RR16439-01 / NCRR NIH HHS S06 GM008102 / NIGMS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000235792500007
- Scopus ID
- 2-s2.0-33644672979
- Other Identifier
- 991014877954604721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology