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@ARTICLE{WickramaArachchilage:22161,
author = {Wickrama Arachchilage, A.P. and Wang, F. and Feyer, V. and
Plekan, O. and Prince, K. C.},
title = {{P}hotoelectron spectra and structures of three cyclic
dipeptides: {P}he{P}he, {T}yr{P}ro and {H}is{G}ly},
journal = {The journal of chemical physics},
volume = {136},
issn = {0021-9606},
address = {Melville, NY},
publisher = {American Institute of Physics},
reportid = {PreJuSER-22161},
pages = {124301},
year = {2012},
note = {We acknowledge the National Computational Infrastructure
(NCI) at the Australian National University for an award
under the Merit Allocation Scheme and Swinburne University
Supercomputing Facilities, and Victorian Partnership for
Advanced Computing (VPAC) for supercomputing facilities.
A.P.W.A. acknowledges a Swinburne University Centenary
Postgraduate Research Award. We thank our colleagues at
Elettra for providing high quality synchrotron light.},
abstract = {We have investigated the electronic structure of three
cyclic dipeptides: cyclo(Histidyl-Glycyl) (cHisGly),
cyclo(Tyrosyl-Prolyl) (cTyrPro), and
cyclo(Phenylalanyl-Phenylalanyl) (cPhePhe) in the vapor
phase, by means of photoemission spectroscopy and
theoretical modeling. The last compound was evaporated from
the solid linear dipeptide, but cyclised, losing water to
form cPhePhe in the gas phase. The results are compared with
our previous studies of three other cyclopeptides.
Experimental valence and core level spectra have been
interpreted in the light of calculations to identify the
basic chemical properties associated with the central
diketopiperazine ring, and with the additional functional
groups. The valence spectra are generally characterized by a
restricted set of outer valence orbitals separated by a gap
from most other valence orbitals. The theoretically
simulated core and valence spectra of all three cyclic
dipeptides agree reasonably well with the experimental
spectra. The central ring and the side chains act as
independent chromophores whose spectra do not influence one
another, except for prolyl dipeptides, where the pyrrole
ring is fused with the central ring. In this case,
significant changes in the valence and core level spectra
were observed, and explained by stronger hybridization of
the valence orbitals.},
keywords = {Computer Simulation / Dipeptides: chemistry / Electrons /
Gases: chemistry / Models, Theoretical / Molecular Structure
/ Peptides, Cyclic: chemistry / Photoelectron Spectroscopy /
Protein Conformation / Dipeptides (NLM Chemicals) / Gases
(NLM Chemicals) / Peptides, Cyclic (NLM Chemicals) /
cyclo(tyrosyl-prolyl) (NLM Chemicals) / histidylglycine (NLM
Chemicals) / cyclo(phenylalanyl-phenylalanyl) (NLM
Chemicals) / J (WoSType)},
cin = {PGI-6},
ddc = {540},
cid = {I:(DE-Juel1)PGI-6-20110106},
pnm = {Grundlagen für zukünftige Informationstechnologien},
pid = {G:(DE-Juel1)FUEK412},
shelfmark = {Physics, Atomic, Molecular $\&$ Chemical},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:22462851},
UT = {WOS:000302216200027},
doi = {10.1063/1.3693763},
url = {https://juser.fz-juelich.de/record/22161},
}