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The infrared and ultraviolet spectra of single conformations of methyl-capped dipeptides: N-acetyl tryptophan amide and N-acetyl tryptophan methyl amide

J. Chem. Phys. 117, 10688 (2002); doi:10.1063/1.1521132

Issue Date: 15 December 2002

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Brian C. Dian, Asier Longarte, and Sebastien Mercier
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907-1393

David A. Evans and David J. Wales
University Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, United Kingdom

Timothy S. Zwier
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907-1393
A combination of methods, including laser-induced fluorescence excitation, fluorescence-dip infrared (FDIR) spectroscopy, and UV-UV hole-burning spectroscopy, have been used to study the infrared and ultraviolet spectra of single conformations of two methyl-capped dipeptides: N-acetyl tryptophan amide (NATA) and N-acetyl tryptophan methyl amide (NATMA). Density functional theory calculations predict that all low-energy conformers of NATA and NATMA belong to one of two conformational families: C5, with its extended dipeptide backbone, or C7eq, in which the dipeptide backbone forms a seven-membered ring joined by a H bond between the psi-amide NH and the phi-amide carbonyl groups. In NATA (NATMA), the LIF spectrum has contributions from two (three) conformers. FDIR spectroscopy has been used to record infrared spectra of the individual conformers over the 2800–3600 cm–1 region, free from interference from one another. The NH stretch region provides unequivocal evidence that one of the conformers of NATA is C5, while the other is C7eq. Similarly, in NATMA, there are two C5 conformers, and one C7eq structure. Several pieces of evidence are used to assign spectra to particular C5 and C7eq conformers. NATA(A) and NATMA(B) are both assigned as C5(AP) structures, NATA(B) and NATMA(C) are assigned as C7eq (PhiP), and NATMA(A) is assigned as C5(APhi). In both molecules, the C5 structures have sharp vibronic spectra, while the C7eq conformers are characterized by a dense, highly congested spectrum involving long progressions that extend several hundred wave numbers to the red of the C5 S1–S0 origins. N-acetyl tryptophan ethyl ester (NATE), which can only form C5 conformers, shows only sharp transitions in its LIF spectrum due to four C5 conformers, with no evidence for the broad absorption due to C7eq. This provides direct experimental evidence for the importance of the peptide backbone conformation in controlling the spectroscopic and photophysical properties of tryptophan. ©2002 American Institute of Physics.
History: Received 30 July 2002; accepted 23 September 2002
Permalink: http://link.aip.org/link/?JCPSA6/117/10688/1
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KEYWORDS and PACS

Keywords
PACS
  • 33.20.Ea
    Molecular properties and interactions with photons Molecular spectra Infrared spectra
  • 33.20.Lg
    Molecular properties and interactions with photons Molecular spectra Ultraviolet spectra
  • 33.50.Dq
    Molecular properties and interactions with photons Fluorescence and phosphorescence; radiationless transitions, quenching (intersystem crossing, internal conversion) Fluorescence and phosphorescence spectra
  • 42.50.Md
    Optics Quantum optics Optical transient phenomena: quantum beats, photon echo, free-induction decay, dephasings and revivals, optical nutation, and self-induced transparency
  • 31.15.Ew
    Electronic structure of atoms and molecules: theory Calculations and mathematical techniques in atomic and molecular physics (excluding electron correlation calculations) Density-functional theory
  • 33.15.Hp
    Molecular properties and interactions with photons Properties of molecules Barrier heights (internal rotation, inversion, rotational isomerism, conformational dynamics)
  • 33.20.Wr
    Molecular properties and interactions with photons Molecular spectra Vibronic, rovibronic, and rotation–electron-spin interactions
  • YEAR: 2002

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0021-9606 (print)   1089-7690 (online)
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