Structural relaxation in the hydrogen-bonding liquids N-methylacetamide and water studied by optical Kerr effect spectroscopy

Turton, D. and Wynne, K. (2008) Structural relaxation in the hydrogen-bonding liquids N-methylacetamide and water studied by optical Kerr effect spectroscopy. Journal of Chemical Physics, 128(15), p. 154516. (doi:10.1063/1.2897432)

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Abstract

Structural relaxation in the peptide model N-methylacetamide (NMA) is studied experimentally by ultrafast optical Kerr effect spectroscopy over the normal-liquid temperature range and compared to the relaxation measured in water at room temperature. It is seen that in both hydrogen-bonding liquids, β relaxation is present, and in each case, it is found that this can be described by the Cole–Cole function. For NMA in this temperature range, the α and β relaxations are each found to have an Arrhenius temperature dependence with indistinguishable activation energies. It is known that the variations on the Debye function, including the Cole–Cole function, are unphysical, and we introduce two general modifications: One allows for the initial rise of the function, determined by the librational frequencies, and the second allows the function to be terminated in the α relaxation.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Wynne, Professor Klaas
Authors: Turton, D., and Wynne, K.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Journal of Chemical Physics
ISSN:0021-9606
Published Online:18 April 2008

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
563561Terahertz spectroscopy of aqueous ionic solutions to understand the role of hydrogen-bond network breaking and strengthening in the HofmeisterKlaas WynneEngineering & Physical Sciences Research Council (EPSRC)EP/E046541/1CHEM - CHEMISTRY