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Structural relaxation in the peptide model N-methylacetamide (NMA) is studiedexperimentally by ultrafast optical Kerr-effect spectroscopy over thenormal-liquid temperature range and compared to the relaxation measured inwater at room temperature. It is seen that in both hydrogen-bonding liquids,beta relaxation is present and in each case it is found that this can bedescribed by the Cole-Cole function. For NMA in this temperature range, thealpha and beta relaxations are each found to have an Arrhenius temperaturedependence with indistinguishable activation energies. It is known that thevariations on the Debye function, including the Cole-Cole function, areunphysical, and we introduce two general modifications: one allows for theinitial rise of the function, determined by the librational frequencies, andthe second allows the function to be terminated in the alpha relaxation.

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