Oligopeptide-based model compounds

The partial molar heat capacity of the glycyl group, Cp(CH2CONH), of a polypeptide has been evaluated in a recent study using partial molar heat capacity data for a series of peptides of amino acid sequence ala(gly) , n = 2-4 [29]. The coefficients a, b, c and d of the polynomial 

The partial molar heat capacities of the amino acid side-chains can be estimated using the partial molar heat capacity data for tripeptides of the form glycyl-X-glycine. The partial molar heat capacity, Cp(R), of any 

Similar to equation 24 the temperature dependence of the partial molar heat capacity of each amino acid side chain can be represented by a third order polynomial. The polynomial coefficients are given in Table 2. 

Side-chain cl (J/molK) b (J/rnolK ) c (J/molK ) lOM (.J/molK ) 

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The applicability of the above approach to the study of intramolecular distances and dynamics has first been demonstrated for a series of flexible oligopeptides (10,15,16). Based on the results obtained for model compounds, the experimental and theoretical methods were applied in a study of protein folding and dynamics. In the following we shall review experiments done towards the investigation of protein denatura-tion and folding by fluorescence labeling and energy transfer measurements. 

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