Stopped-flow studies of the N ⇌ F transition in serum albumin

Ronald P. Taylor, Vincent Chau, Mathew J. Zenkowich, Luther H. Leake

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Stopped-flow studies of the refolding of iodoacetamide-blocked bovine serum albumin from the acid unfolded "F" state have been performed. If the protein is incubated with low concentrations of perchlorate anion then the refolding kinetics follow a simple first-order process. The dependence on pH of both the amplitude of the observed transients and the measured rate constants indicates that the N ⇌ F transition is highly cooperative. The results are consistent with the postulated multidomain structure of albumin which has been developed as a result of both sequence work and a variety of physical studies.

Original languageEnglish (US)
Pages (from-to)293-299
Number of pages7
JournalBiophysical Chemistry
Volume7
Issue number4
DOIs
StatePublished - Jan 1978

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Organic Chemistry

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