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, Charles Angell, Pablo G. Debenedetti

Research output: Contribution to journalArticle

9 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)4441-4443
Number of pages3
JournalChemical Communications
Issue number29
DOIs
StatePublished - 2009

Fingerprint

Protein folding
Muramidase
Infrared spectroscopy
Quenching
Enzymes
Proteins
Scanning
Experiments
Temperature

ASJC Scopus subject areas

  • Metals and Alloys
  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Catalysis
  • Chemistry(all)

Cite this

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, Charles; Debenedetti, Pablo G.

In: Chemical Communications, No. 29, 2009, p. 4441-4443.

Research output: Contribution to journalArticle

Cho, Theresa Y. ; Byrne, Nolene ; Moore, David J. ; Pethica, Brian A. ; Angell, Charles ; Debenedetti, Pablo G. / Structure-energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state. In: Chemical Communications. 2009 ; No. 29. pp. 4441-4443.
@article{07163b5ea3784c7dbfe6c639efeb1a08,
title = "Structure-energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state",
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 Charles Angell and Debenedetti, {Pablo G.}",
year = "2009",
doi = "10.1039/b907656e",
language = "English (US)",
pages = "4441--4443",
journal = "Chemical Communications (London)",
issn = "1359-7345",
publisher = "Royal Society of Chemistry",
number = "29",

}

TY - JOUR

T1 - Structure-energy relations in hen egg white lysozyme observed during refolding from a quenched unfolded state

AU - Cho, Theresa Y.

AU - Byrne, Nolene

AU - Moore, David J.

AU - Pethica, Brian A.

AU - Angell, Charles

AU - Debenedetti, Pablo G.

PY - 2009

Y1 - 2009

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=70249085617&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=70249085617&partnerID=8YFLogxK

U2 - 10.1039/b907656e

DO - 10.1039/b907656e

M3 - Article

C2 - 19597619

AN - SCOPUS:70249085617

SP - 4441

EP - 4443

JO - Chemical Communications (London)

JF - Chemical Communications (London)

SN - 1359-7345

IS - 29

ER -