Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 degrees C.

Autor: Häckel M; Institut für Physikalische Chemie der Westfälischen Wilhelms-Universität Münster, Schlossplatz 4-7, D-48149 Münster, Germany., Hinz HJ, Hedwig GR
Jazyk: angličtina
Zdroj: Biophysical chemistry [Biophys Chem] 1999 Nov 15; Vol. 82 (1), pp. 35-50.
DOI: 10.1016/s0301-4622(99)00104-0
Abstrakt: The partial molar volumes of tripeptides of sequence glycyl-X-glycine, where X is one of the amino acids alanine, leucine, threonine, glutamine, phenylalanine, histidine, cysteine, proline, glutamic acid, and arginine, have been determined in aqueous solution over the temperature range 10-90 degrees C using differential scanning densitometry . These data, together with those reported previously, have been used to derive the partial molar volumes of the side-chains of all 20 amino acids. The side-chain volumes are critically compared with literature values derived using partial molar volumes for alternative model compounds. The new amino acid side-chain volumes, along with that for the backbone glycyl group, were used to calculate the partial specific volumes of several proteins in aqueous solution. The results obtained are compared with those observed experimentally. The new side-chain volumes have also been used to re-determine residue volume changes upon protein folding.
Databáze: MEDLINE