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

Access to Document

10.1039/b003768k

Cite this

Colley, C. S., Clark, I. P., Griffiths-Jones, S. R., George, M. W., & Searle, M. S. (2000). 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. Chemical Communications, (16), 1493-1494. https://doi.org/10.1039/b003768k

@article{d895a1d634694f5ba12d6bd2b679dbe0,

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",

number = "16",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0034699075&partnerID=8YFLogxK

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

Access to Document

Other files and links

Fingerprint

Cite this