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

Cho, Theresa Y., Byrne, Nolene, Moore, David J., Pethica, Brian A., Angell, C. Austen and Debenedetti, Pablo G. 2009, Structure–energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state, Chemical communications, vol. 29, pp. 4441-4443, doi: 10.1039/B907656E.

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Title Structure–energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state
Author(s) Cho, Theresa Y.
Byrne, NoleneORCID iD for Byrne, Nolene orcid.org/0000-0002-9474-7644
Moore, David J.
Pethica, Brian A.
Angell, C. Austen
Debenedetti, Pablo G.
Journal name Chemical communications
Volume number 29
Start page 4441
End page 4443
Total pages 3
Publisher Royal Society of Chemistry
Place of publication Cambridge, England
Publication date 2009
ISSN 1359-7345
1364-548X
Summary 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.
Language eng
DOI 10.1039/B907656E
Field of Research 039999 Chemical Sciences not elsewhere classified
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2009, Royal Society of Chemistry
Persistent URL http://hdl.handle.net/10536/DRO/DU:30039454

Document type: Journal Article
Collections: Centre for Material and Fibre Innovation
GTP Research
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Created: Wed, 26 Oct 2011, 09:02:24 EST

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