Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH

C. S. Colley, I. P. Clark, S. R. Griffiths-Jones, M. W. George, M. S. Searle

Research output: Journal PublicationArticlepeer-review

16 Citations (Scopus)

Abstract

Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH ~ 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of ~ 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.

Original languageEnglish
Pages (from-to)1493-1494
Number of pages2
JournalChemical Communications
Issue number16
DOIs
Publication statusPublished - 21 Aug 2000
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry (all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Fingerprint

Dive into the research topics of 'Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH'. Together they form a unique fingerprint.

Cite this