Journal article
Conformations of alanine-based peptides in water probed by FTIR, Raman, vibrational circular dichroism, electronic circular dichroism, and NMR spectroscopy
Biochemistry (Easton), v 46(6), pp 1587-1596
13 Feb 2007
PMID: 17279623
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
We have used a combination of FTIR, VCD, ECD, Raman, and NMR spectroscopies to probe the solution conformations sampled by H-(AAKA)-OH by utilizing an excitonic coupling model and constraints imposed by the 3JCalphaHNH coupling constants of the central residues to simulate the amide I' profile of the IR, isotropic Raman, anisotropic Raman, and VCD spectra in terms of a mixture of three conformations, i.e., polyproline II, beta-strand and right-handed helical. The representative coordinates of the three conformations were obtained from published coil libraries. Alanine was found to exhibit PPII fractions of 0.60 or greater, mixed with smaller fractions of helices and beta-strand conformations. Lysine showed no clear conformational propensity in that it samples polyproline II, beta-strand, and helical conformations with comparable probability. This is at variance with results obtained earlier for ionized polylysine, which suggest a high polyproline II propensity. We reanalyzed previously investigated tetra- and trialanine by combining published vibrational spectroscopy data with 3JCalphaHNH coupling constants and obtained again blends dominated by PPII with smaller admixtures of beta-strand and right-handed helical conformations. The polyproline II propensity of alanine was found to be higher in tetraalanine than in trialanine. For all peptides investigated, our results rule out a substantial population of turn-like conformations. Our results are in excellent agreement with MD simulations on short alanine peptides by Gnanakaran and Garcia [(2003) J. Phys. Chem. B 107, 12555-12557] but at variance with multiple MD simulations particularly for the alanine dipeptide.
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Details
- Title
- Conformations of alanine-based peptides in water probed by FTIR, Raman, vibrational circular dichroism, electronic circular dichroism, and NMR spectroscopy
- Creators
- Reinhard Schweitzer-Stenner - Department of Chemistry, Drexel University, Philadelphia, Pennsylvania 19104, USA. RSchweitzer-Stenner@drexel.eduThomas MeaseyLazaros KakalisFrank JordanSilvia PizzanelliClaudia ForteKai Griebenow
- Publication Details
- Biochemistry (Easton), v 46(6), pp 1587-1596
- Publisher
- American Chemical Society; Washington, DC
- Grant note
- P20 RR16439-01 / NCRR NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000243989500014
- Scopus ID
- 2-s2.0-33847029566
- Other Identifier
- 991014878595504721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology