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

Theresa Y. Cho; Nolene Byrne; David J. Moore; Brian A. Pethica; C. Austen Angell; Pablo G. Debenedetti

doi:10.1039/b907656e

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

Theresa Y. Cho, Nolene Byrne, David J. Moore, Brian A. Pethica, C. Austen Angell, Pablo G. Debenedetti

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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.

Original language	English (US)
Pages (from-to)	4441-4443
Number of pages	3
Journal	Chemical Communications
Issue number	29
DOIs	https://doi.org/10.1039/b907656e
State	Published - 2009

All Science Journal Classification (ASJC) codes

Electronic, Optical and Magnetic Materials
General Chemistry
Ceramics and Composites
Metals and Alloys
Materials Chemistry
Surfaces, Coatings and Films
Catalysis

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10.1039/b907656e

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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.",

author = "Cho, {Theresa Y.} and Nolene Byrne and Moore, {David J.} and Pethica, {Brian A.} and {Austen Angell}, C. and Debenedetti, {Pablo G.}",

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AU - Cho, Theresa Y.

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AU - Moore, David J.

AU - Pethica, Brian A.

AU - Austen Angell, C.

AU - Debenedetti, Pablo G.

PY - 2009

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AB - 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.

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JO - Chemical Communications

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

Abstract

All Science Journal Classification (ASJC) codes

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