Characterization of low-frequency modes in aqueous peptides using far-infrared spectroscopy and molecular dynamics simulation

Ding, Tao, Huber, Thomas, Middelberg, Anton P. J. and Falconer, Robert J. (2011) Characterization of low-frequency modes in aqueous peptides using far-infrared spectroscopy and molecular dynamics simulation. The Journal of Physical Chemistry Part A, 115 42: 11559-11565. doi:10.1021/jp200553d


Author Ding, Tao
Huber, Thomas
Middelberg, Anton P. J.
Falconer, Robert J.
Title Characterization of low-frequency modes in aqueous peptides using far-infrared spectroscopy and molecular dynamics simulation
Journal name The Journal of Physical Chemistry Part A   Check publisher's open access policy
ISSN 1089-5639
1520-5215
Publication date 2011-10-01
Sub-type Article (original research)
DOI 10.1021/jp200553d
Volume 115
Issue 42
Start page 11559
End page 11565
Total pages 7
Place of publication Washington, DC, United States
Publisher American Chemical Society
Collection year 2012
Language eng
Formatted abstract
Far-infrared spectroscopy was used to study the dynamics of three aqueous peptides having varied helicity. Experimental data were compared to the molecular dynamics simulated far-infrared absorbance spectrum derived from the dipole time correlation function. Vibrational density of state (VDOS) simulation was then used to analyze the contribution of different structural elements to the bands. Frozen aqueous peptide samples were studied in the frequency range between 325 and 540 cm -1 where the ice absorbance is low. Three resonances were identified; band I centered at approximately 333 cm -1, band II centered at approximately 380 cm -1, and band III comprising two constituent bands at approximately 519 and 528 cm -1. The peak height and frequency of the maximum absorbance of bands I and II varied depending on the helicity of the peptide. VDOS of the far-infrared absorbance spectrum confirmed that bands I and II were associated with the peptide backbone and that band III had both potential backbone and side chain components.
Keyword Protein Secondary Structure
Vibrational Analysis
Liquid Water
Circular-Dichroism
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
Australian Institute for Bioengineering and Nanotechnology Publications
 
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