Fast events in protein folding: Helix melting and formation in a small peptide

Skip Williams, Timothy P. Causgrove, Rudolf Gilmanshin, Karen S. Fang, Robert Callender, William H. Woodruff, R. Brian Dyer

Research output: Contribution to journalArticle

569 Citations (Scopus)

Abstract

The helix is a common secondary structural motif found in proteins, and the mechanism of helix-coil interconversion is key to understanding the protein-folding problem. We report the observation of the fast kinetics (nanosecond to millisecond) of helix melting in a small 21-residue alanine- based peptide. The unfolding reaction is initiated using a laser-induced temperature jump and probed using time-resolved infrared spectroscopy. The model peptide exhibits fast unfolding kinetics with a time constant of 160 ± 60 ns at 28 °C in response to a laser-induced temperature jump of 18 °C which is completed within 20 ns. Using the unfolding time and the measured helix-coil equilibrium constant of the model peptide, a folding rate constant of approximately 6 x 10 7 s -1 (t( 1/2 ) = 16 ns) can be inferred for the helix formation reaction at 28 °C. These results demonstrate that secondary structure formation is fast enough to be a key event at early times in the protein-folding process and that helices are capable of forming before long range tertiary contacts are made.

Original languageEnglish (US)
Pages (from-to)691-697
Number of pages7
JournalBiochemistry
Volume35
Issue number3
DOIs
StatePublished - Jan 23 1996
Externally publishedYes

Fingerprint

Protein folding
Protein Folding
Freezing
Melting
Peptides
Lasers
Kinetics
Equilibrium constants
Alanine
Temperature
Infrared spectroscopy
Rate constants
Spectrum Analysis
Observation
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Williams, S., Causgrove, T. P., Gilmanshin, R., Fang, K. S., Callender, R., Woodruff, W. H., & Dyer, R. B. (1996). Fast events in protein folding: Helix melting and formation in a small peptide. Biochemistry, 35(3), 691-697. https://doi.org/10.1021/bi952217p

Fast events in protein folding : Helix melting and formation in a small peptide. / Williams, Skip; Causgrove, Timothy P.; Gilmanshin, Rudolf; Fang, Karen S.; Callender, Robert; Woodruff, William H.; Dyer, R. Brian.

In: Biochemistry, Vol. 35, No. 3, 23.01.1996, p. 691-697.

Research output: Contribution to journalArticle

Williams, S, Causgrove, TP, Gilmanshin, R, Fang, KS, Callender, R, Woodruff, WH & Dyer, RB 1996, 'Fast events in protein folding: Helix melting and formation in a small peptide', Biochemistry, vol. 35, no. 3, pp. 691-697. https://doi.org/10.1021/bi952217p
Williams S, Causgrove TP, Gilmanshin R, Fang KS, Callender R, Woodruff WH et al. Fast events in protein folding: Helix melting and formation in a small peptide. Biochemistry. 1996 Jan 23;35(3):691-697. https://doi.org/10.1021/bi952217p
Williams, Skip ; Causgrove, Timothy P. ; Gilmanshin, Rudolf ; Fang, Karen S. ; Callender, Robert ; Woodruff, William H. ; Dyer, R. Brian. / Fast events in protein folding : Helix melting and formation in a small peptide. In: Biochemistry. 1996 ; Vol. 35, No. 3. pp. 691-697.
@article{1b63e3ae37434456b10cd80b06ad2be0,
title = "Fast events in protein folding: Helix melting and formation in a small peptide",
abstract = "The helix is a common secondary structural motif found in proteins, and the mechanism of helix-coil interconversion is key to understanding the protein-folding problem. We report the observation of the fast kinetics (nanosecond to millisecond) of helix melting in a small 21-residue alanine- based peptide. The unfolding reaction is initiated using a laser-induced temperature jump and probed using time-resolved infrared spectroscopy. The model peptide exhibits fast unfolding kinetics with a time constant of 160 ± 60 ns at 28 °C in response to a laser-induced temperature jump of 18 °C which is completed within 20 ns. Using the unfolding time and the measured helix-coil equilibrium constant of the model peptide, a folding rate constant of approximately 6 x 10 7 s -1 (t( 1/2 ) = 16 ns) can be inferred for the helix formation reaction at 28 °C. These results demonstrate that secondary structure formation is fast enough to be a key event at early times in the protein-folding process and that helices are capable of forming before long range tertiary contacts are made.",
author = "Skip Williams and Causgrove, {Timothy P.} and Rudolf Gilmanshin and Fang, {Karen S.} and Robert Callender and Woodruff, {William H.} and Dyer, {R. Brian}",
year = "1996",
month = "1",
day = "23",
doi = "10.1021/bi952217p",
language = "English (US)",
volume = "35",
pages = "691--697",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "3",

}

TY - JOUR

T1 - Fast events in protein folding

T2 - Helix melting and formation in a small peptide

AU - Williams, Skip

AU - Causgrove, Timothy P.

AU - Gilmanshin, Rudolf

AU - Fang, Karen S.

AU - Callender, Robert

AU - Woodruff, William H.

AU - Dyer, R. Brian

PY - 1996/1/23

Y1 - 1996/1/23

N2 - The helix is a common secondary structural motif found in proteins, and the mechanism of helix-coil interconversion is key to understanding the protein-folding problem. We report the observation of the fast kinetics (nanosecond to millisecond) of helix melting in a small 21-residue alanine- based peptide. The unfolding reaction is initiated using a laser-induced temperature jump and probed using time-resolved infrared spectroscopy. The model peptide exhibits fast unfolding kinetics with a time constant of 160 ± 60 ns at 28 °C in response to a laser-induced temperature jump of 18 °C which is completed within 20 ns. Using the unfolding time and the measured helix-coil equilibrium constant of the model peptide, a folding rate constant of approximately 6 x 10 7 s -1 (t( 1/2 ) = 16 ns) can be inferred for the helix formation reaction at 28 °C. These results demonstrate that secondary structure formation is fast enough to be a key event at early times in the protein-folding process and that helices are capable of forming before long range tertiary contacts are made.

AB - The helix is a common secondary structural motif found in proteins, and the mechanism of helix-coil interconversion is key to understanding the protein-folding problem. We report the observation of the fast kinetics (nanosecond to millisecond) of helix melting in a small 21-residue alanine- based peptide. The unfolding reaction is initiated using a laser-induced temperature jump and probed using time-resolved infrared spectroscopy. The model peptide exhibits fast unfolding kinetics with a time constant of 160 ± 60 ns at 28 °C in response to a laser-induced temperature jump of 18 °C which is completed within 20 ns. Using the unfolding time and the measured helix-coil equilibrium constant of the model peptide, a folding rate constant of approximately 6 x 10 7 s -1 (t( 1/2 ) = 16 ns) can be inferred for the helix formation reaction at 28 °C. These results demonstrate that secondary structure formation is fast enough to be a key event at early times in the protein-folding process and that helices are capable of forming before long range tertiary contacts are made.

UR - http://www.scopus.com/inward/record.url?scp=0030046906&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030046906&partnerID=8YFLogxK

U2 - 10.1021/bi952217p

DO - 10.1021/bi952217p

M3 - Article

C2 - 8547249

AN - SCOPUS:0030046906

VL - 35

SP - 691

EP - 697

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 3

ER -