Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range
✍ Scribed by G. I. Makhatadze; V. N. Medvedkin; P. L. Privalov
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1990
- Tongue
- English
- Weight
- 644 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
The partial molar volumes of various compounds that model protein constituent groups, such as tripeptides (Gly-X-Gly, where X = Gly, Ala, Val, Leu, Ile, Pro, Met, His, Ser), homopeptides (Gly,, n = 3, 4, 5 ) , and simple organic analogues of amino acid side chains (methanol, acetamide, propanamide, acetic acid, propanoic acid, n -butanamine, n-butanamine nitrate, n -propylguanidine nitrate, 4-methylphenol ) , have been determined in aqueous solution with a vibrational densimeter in the temperature range of 5-85°C. The partial molar volumes of amino acid side chains and the peptide unit were estimated from the data obtained. Assuming additivity of component groups, the partial molar volumes of polypeptide chains of several proteins over a broad temperature range were calculated. The partial molar volume functions of four proteins ( myoglobin, cytochrome C, ribonuclease A, lysozyme) were compared with those determined experimentally for the unfolded and native forms of these proteins. It has been shown that the average deviation of the calculated functions from the experimental ones does not exceed 3% over the temperature range studied.
' -0Pfp H L O B 2 1 0 ~2 1 Figure 1. Reaction scheme for the synthesis of tripeptides.