Partial specific volumes of synthetic polypeptides in dilute solution
✍ Scribed by C. De Loźe; P. Saludjian; A. J. Kovacs; B. Schermutzki
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1964
- Tongue
- English
- Weight
- 336 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
We report a simple method for measuring partial specific volumes. of polymers in This method has been ap-The residue volumes deduced from these
The discrepancy is dilute solutions with an accuracy of 3 parts per thousand.
plied to 7 polypeptides in 4 organic solvents.
data are compared to those calculated by a differential method. generally of the order of 1.5%.
📜 SIMILAR VOLUMES
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,
Partial spec$c uolumes at 25°C are reported for a-chymotrypsinogen in aqueous solutions containing NaCI, citrate, and/or polyethylene glycol (PEG) ouer a range of protein concentrations. The concentration dependence of the partial specific uolume can be either positive or negatiue, depending on the
## Abstract Helix–coil transitions of poly(ε‐carbobenzyloxy L‐lysine) (PCBL) in __m__‐cresol and in mixtures of dichloroacetic acid (DCA) and ethylene dichloride (EDC) were investigated by optical rotation measurements, with special interest in the molecular‐weight dependence of helical content. Th
Simple approximate expressions have been derived from the theory of Zimm and Bragg for use in the analysis of experimental data on the helix-coil transition in polypeptide. On the basis of the resulting expressions practical procedures are proposed t o determine two basic parameters characterizing a