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 articlepeer-review

    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

    Fingerprint

    Dive into the research topics of 'Aqueous interfacial driving forces in the folding and assembly of protein (elastin)-based polymers. Differential scanning calorimetry studies'. Together they form a unique fingerprint.

    Cite this