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

Authors
Colley, CS Clark, IP Griffiths-Jones, SR George, MW Searle, MS
Citation
Cs. Colley et al., 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, CHEM COMMUN, (16), 2000, pp. 1493-1494
Citations number
33
Categorie Soggetti
Chemistry
Journal title
CHEMICAL COMMUNICATIONS
ISSN journal
13597345 → ACNP
Issue
16
Year of publication
2000
Pages
1493 - 1494
Database
ISI
SICI code
1359-7345(2000):16<1493:SSATIS>2.0.ZU;2-I
Abstract
Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic c onditions (pH similar to 1); fast time-resolved measurements of protein unf olding, initiated by a laser-induced temperature-jump of similar to 8 degre es C, shows rapid refolding and beta-sheet secondary structure formation on a timescale of a few milliseconds.