Aqueous interfacial driving forces in the folding and assembly of protein (elastin)-based polymers. Differential scanning calorimetry studies

D. W. Urry*, C. H. Luan, R. D. Harris, K. U. Prasad

*Corresponding author for this work

Research output: Contribution to journalConference article

17 Scopus citations

Abstract

The protein element of interest here is poly[4(VPGVG), (VPGEG)] in which there are, on the average, four Glu residues per 100 residues. The transition seen as chemomechanical transduction in the cross-linked matrix is seen before cross-linking as a transition from a solution at low temperature to aggregation and phase separation on raising the temperature above that of the transition. The more dense viscoelastic phase formed, called the coacervate, is about 400 mg polypeptide/ml (40% peptide, 60% water by weight). In the present report differential scanning calorimetry is used to determine the heats of the transition (heats of coacervation) as a function of pH.

Original languageEnglish (US)
Pages (from-to)188-189
Number of pages2
JournalAmerican Chemical Society, Polymer Preprints, Division of Polymer Chemistry
Volume31
Issue number1
StatePublished - Apr 1 1990
EventPapers Presented at the Boston, Massachusetts Meeting of ACS 1989 - Boston, MA, USA
Duration: Apr 22 1989Apr 27 1989

ASJC Scopus subject areas

  • Polymers and Plastics

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