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 journalArticle

5 Citations (Scopus)

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 1 1978

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Iodoacetamide
Bovine Serum Albumin
Serum Albumin
Anions
Albumins
Rate constants
Kinetics
Acids
Proteins
perchlorate

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Organic Chemistry

Cite this

Taylor, Ronald P. ; Chau, Vincent ; Zenkowich, Mathew J. ; Leake, Luther H. / Stopped-flow studies of the N ⇌ F transition in serum albumin. In: Biophysical Chemistry. 1978 ; Vol. 7, No. 4. pp. 293-299.
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Stopped-flow studies of the N ⇌ F transition in serum albumin. / Taylor, Ronald P.; Chau, Vincent; Zenkowich, Mathew J.; Leake, Luther H.

In: Biophysical Chemistry, Vol. 7, No. 4, 01.01.1978, p. 293-299.

Research output: Contribution to journalArticle

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