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Partial Molar Isentropic Compressions of Some Tetra- and Pentapeptides in Aqueous Solution: Implications for Group Additivity Schemes for Unfolded Proteins

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Abstract

Sound speeds have been measured for aqueous solutions of five tetrapeptides and five pentapeptides at T=298.15 K. The partial molar isentropic compressions at infinite dilution, \(K_{S,2}^{\circ}\), were derived for the peptides using conventional methods. The results were compared with those calculated using group additivity methods, with the amino acid side-chain contributions derived using \(K_{S,2}^{\circ}\) data reported previously for some tripeptides of sequence gly-X-gly, where X represents an amino acid, and also for some N-acetyl amino acid amides. The tripeptides are the preferred model compounds for the estimation of the side-chain contributions to \(K_{S,2}^{\circ}\) of a polypeptide. Our study also confirms that simple group additivity schemes are not feasible for the estimation of \(K_{S,2}^{\circ}\) values for polypeptides and unfolded proteins.

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Acknowledgements

We thank Einar Høgseth for his technical expertise in the design and maintenance of the speed of sound equipment.

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Authors and Affiliations

  1. Institute of Fundamental Sciences-Chemistry, Massey University, Private Bag 11 222, Palmerston North, New Zealand

    Gavin R. Hedwig

  2. Department of Chemistry, University of Bergen, 5020, Bergen, Norway

    Harald Høiland

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  1. Gavin R. Hedwig
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  2. Harald Høiland
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Correspondence to Gavin R. Hedwig.

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Hedwig, G.R., Høiland, H. Partial Molar Isentropic Compressions of Some Tetra- and Pentapeptides in Aqueous Solution: Implications for Group Additivity Schemes for Unfolded Proteins. J Solution Chem 41, 690–701 (2012). https://doi.org/10.1007/s10953-012-9818-3

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