Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH

C. S. Colley; I. P. Clark; S. R. Griffiths-Jones; M. W. George; M. S. Searle

doi:10.1039/b003768k

Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH

C. S. Colley, I. P. Clark, S. R. Griffiths-Jones, M. W. George, M. S. Searle

Research output: Journal Publication › Article › peer-review

16 Citations (Scopus)

Abstract

Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH ~ 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of ~ 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.

Original language	English
Pages (from-to)	1493-1494
Number of pages	2
Journal	Chemical Communications
Issue number	16
DOIs	https://doi.org/10.1039/b003768k
Publication status	Published - 21 Aug 2000
Externally published	Yes

ASJC Scopus subject areas

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

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10.1039/b003768k

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title = "Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH",

abstract = "Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH ~ 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of ~ 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.",

author = "Colley, {C. S.} and Clark, {I. P.} and Griffiths-Jones, {S. R.} and George, {M. W.} and Searle, {M. S.}",

year = "2000",

month = aug,

day = "21",

doi = "10.1039/b003768k",

language = "English",

pages = "1493--1494",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

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Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH. / Colley, C. S.; Clark, I. P.; Griffiths-Jones, S. R. et al.
In: Chemical Communications, No. 16, 21.08.2000, p. 1493-1494.

Research output: Journal Publication › Article › peer-review

TY - JOUR

T1 - Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin

T2 - Protein stability and temperature-jump kinetic measurements of protein folding at low pH

AU - Colley, C. S.

AU - Clark, I. P.

AU - Griffiths-Jones, S. R.

AU - George, M. W.

AU - Searle, M. S.

PY - 2000/8/21

Y1 - 2000/8/21

N2 - Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH ~ 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of ~ 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.

AB - Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH ~ 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of ~ 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.

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U2 - 10.1039/b003768k

DO - 10.1039/b003768k

M3 - Article

AN - SCOPUS:0034699075

SN - 1359-7345

SP - 1493

EP - 1494

JO - Chemical Communications

JF - Chemical Communications

IS - 16

ER -

Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH

Abstract

ASJC Scopus subject areas

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