Issue 16, 2000
From the journal:

Chemical Communications

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

Christopher S. Colley,a   Ian P. Clark,b   Samuel R. Griffiths-Jones,a   Michael W. George*a  and  Mark S. Searle*a  

* Corresponding authors

a Department of Chemistry, University Park, Nottingham, UK
E-mail: mark.searle@nottingham.ac.uk, mike.george@nottingham.ac.uk

b Central Laser Facility, Rutherford Appleton Laboratory, Chilton, Didcot, Oxfordshire, UK

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.

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Article information

DOI
https://doi.org/10.1039/B003768K
Article type
Communication
Submitted
11 May 2000
Accepted
19 Jun 2000
First published
19 Jul 2000

Chem. Commun., 2000, 1493-1494

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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 and M. S. Searle, Chem. Commun., 2000, 1493 DOI: 10.1039/B003768K

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