Author(s): BarberArmstrong W, Donaldson T, Wijesooriya H, Silva RA, Decatur SM, BarberArmstrong W, Donaldson T, Wijesooriya H, Silva RA, Decatur SM, BarberArmstrong W, Donaldson T, Wijesooriya H, Silva RA, Decatur SM, BarberArmstrong W, Donaldson T, Wijesooriya H, Silva RA, Decatur SM
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Abstract Infrared spectroscopy (IR) is commonly used to study secondary structure of both peptides and proteins. The amide I band is very sensitive to peptide secondary structure, and the conformation of a peptide can be probed at the residue level by introducing site-specific isotope-labels into the peptide backbone. The replacement of a carbonyl (12)C with a (13)C results in a approximately 40 cm(-1) shift in the amide I' band. The amide I bands of specifically labeled helices should vary systematically as a function of the number and relative spacing of the labeled residues; thus one should be able to describe the conformation of a polypeptide in substantial detail by probing the changes in IR spectra as a function of the number and positioning of isotope labels. In this study, we report IR spectra of a series of differently labeled helical peptides. A series of 25mer peptides were synthesized based on the repeat sequence (AAAAK)(n). We have varied the number and spacing of the labels on each peptide and studied the changes in the (12)C and (13)C amide I' band due to label position. Our results indicate that changing the number of labels changes the frequency and intensity of both the (12)C and the (13)C amide mode. We also found that varying the spacing between labels causes these amide peaks to shift. Isotope labeling, combined with IR spectroscopy and theoretical predictions, may generate a description of peptide backbone conformations at the residue level.
This article was published in J Am Chem Soc
and referenced in Journal of Physical Chemistry & Biophysics