Issue 29, 2009
From the journal:

Chemical Communications

Structure–energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state†

Theresa Y. Cho,a   Nolene Byrne,b   David J. Moore,c   Brian A. Pethica,a   C. Austen Angellb  and  Pablo G. Debenedetti*a  

* Corresponding authors

a Department of Chemical Engineering, Princeton University, Princeton, USA
E-mail: pdebene@princeton.edu
Fax: +1 609 258 0211
Tel: +1 609 258 5480

b Department of Chemistry and Biochemistry, Arizona State University, Tempe, USA

c International Specialty Products, 1361 Alps Road, Wayne, USA

Abstract

We use infrared spectroscopy to study the evolution of protein folding intermediate structures on arbitrarily slow time scales by rapidly quenching thermally unfolded hen egg white lysozyme in a glassy matrix, followed by reheating of the protein to refold; upon comparison with differential scanning calorimetric experiments, low-temperature structural changes that precede the formation of energetic native contacts are revealed.

Graphical abstract: Structure–energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state

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Article information

DOI
https://doi.org/10.1039/B907656E
Article type
Communication
Submitted
16 Apr 2009
Accepted
18 May 2009
First published
12 Jun 2009

Chem. Commun., 2009, 4441-4443

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Structure–energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state

T. Y. Cho, N. Byrne, D. J. Moore, B. A. Pethica, C. Austen Angell and P. G. Debenedetti, Chem. Commun., 2009, 4441 DOI: 10.1039/B907656E

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