Structure–energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state
Data(s) |
01/01/2009
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Resumo |
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.<br /> |
Identificador | |
Idioma(s) |
eng |
Publicador |
Royal Society of Chemistry |
Relação |
http://dro.deakin.edu.au/eserv/DU:30039454/byrne-structure-2009.pdf http://dx.doi.org/10.1039/B907656E |
Direitos |
2009, Royal Society of Chemistry |
Tipo |
Journal Article |