http://www.cnr.it/ontology/cnr/individuo/prodotto/ID39795
Conformations of Alanine-Based Peptides in Water Probed by FTIR, Raman, Vibrational Circular Dichroism, Electronic Circular Dichroism, and NMR Spectroscopy (Articolo in rivista)
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- Conformations of Alanine-Based Peptides in Water Probed by FTIR, Raman, Vibrational Circular Dichroism, Electronic Circular Dichroism, and NMR Spectroscopy (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/bi062224l (literal)
- Alternative label
Schweitzer-Stenner Reinhard; Thomas Measey; Lazaros Kakalis; Frank Jordan; Silvia Pizzanelli; Claudia Forte; Kai Griebenow (2007)
Conformations of Alanine-Based Peptides in Water Probed by FTIR, Raman, Vibrational Circular Dichroism, Electronic Circular Dichroism, and NMR Spectroscopy
in Biochemistry (Easton)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Schweitzer-Stenner Reinhard; Thomas Measey; Lazaros Kakalis; Frank Jordan; Silvia Pizzanelli; Claudia Forte; Kai Griebenow (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Department of Chemistry, Drexel University, Philadelphia, PA, USA
Department of Chemistry, Rutgers University, Newark, NJ, USA
Istituto per i Processi Chimico-Fisici, CNR, Pisa, Italy
Department of Chemistry, University of Puerto Rico, San Juan, PR (literal)
- Titolo
- Conformations of Alanine-Based Peptides in Water Probed by FTIR, Raman, Vibrational Circular Dichroism, Electronic Circular Dichroism, and NMR Spectroscopy (literal)
- 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 3JCáHNH coupling constants of the central residues to simulate the amide I profile of the IR, isotropic Raman, anisotropic Raman and VCD spectrum 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 earlier results obtained for ionized polylysine, which suggest a high polyproline II propensity. We reanalyzed previously investigated tetra- and trialanine by combining published vibrational spectroscopy data with 3JCalfaHNH 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 (J. Phys. Chem. B. 2003, 107, 12555-12557), but at variance with multiple MD simulations particularly for the alanine dipeptide. (literal)
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