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Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.

Publication ,  Journal Article
Dimitriadis, G; Drysdale, A; Myers, JK; Arora, P; Radford, SE; Oas, TG; Smith, DA
Published in: Proc Natl Acad Sci U S A
March 16, 2004

The small size (58 residues) and simple structure of the B domain of staphylococcal protein A (BdpA) have led to this domain being a paradigm for theoretical studies of folding. Experimental studies of the folding of BdpA have been limited by the rapidity of its folding kinetics. We report the folding kinetics of a fluorescent mutant of BdpA (G29A F13W), named F13W*, using nanosecond laser-induced temperature jump experiments. Automation of the apparatus has permitted large data sets to be acquired that provide excellent signal-to-noise ratio over a wide range of experimental conditions. By measuring the temperature and denaturant dependence of equilibrium and kinetic data for F13W*, we show that thermodynamic modeling of multidimensional equilibrium and kinetic surfaces is a robust method that allows reliable extrapolation of rate constants to regions of the folding landscape not directly accessible experimentally. The results reveal that F13W* is the fastest-folding protein of its size studied to date, with a maximum folding rate constant at 0 M guanidinium chloride and 45 degrees C of 249,000 s(-1). Assuming the single-exponential kinetics represent barrier-limited folding, these data limit the value for the preexponential factor for folding of this protein to at least approximately 2 x 10(6) s(-1).

Duke Scholars

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

March 16, 2004

Volume

101

Issue

11

Start / End Page

3809 / 3814

Location

United States

Related Subject Headings

  • Staphylococcal Protein A
  • Spectrum Analysis
  • Protein Structure, Tertiary
  • Protein Folding
  • Mutation
  • Lasers
  • Hot Temperature
  • Amino Acid Substitution
 

Citation

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Dimitriadis, G., Drysdale, A., Myers, J. K., Arora, P., Radford, S. E., Oas, T. G., & Smith, D. A. (2004). Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump. Proc Natl Acad Sci U S A, 101(11), 3809–3814. https://doi.org/10.1073/pnas.0306433101
Dimitriadis, George, Adam Drysdale, Jeffrey K. Myers, Pooja Arora, Sheena E. Radford, Terence G. Oas, and D Alastair Smith. “Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.Proc Natl Acad Sci U S A 101, no. 11 (March 16, 2004): 3809–14. https://doi.org/10.1073/pnas.0306433101.
Dimitriadis G, Drysdale A, Myers JK, Arora P, Radford SE, Oas TG, et al. Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump. Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3809–14.
Dimitriadis, George, et al. “Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.Proc Natl Acad Sci U S A, vol. 101, no. 11, Mar. 2004, pp. 3809–14. Pubmed, doi:10.1073/pnas.0306433101.
Dimitriadis G, Drysdale A, Myers JK, Arora P, Radford SE, Oas TG, Smith DA. Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump. Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3809–3814.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

March 16, 2004

Volume

101

Issue

11

Start / End Page

3809 / 3814

Location

United States

Related Subject Headings

  • Staphylococcal Protein A
  • Spectrum Analysis
  • Protein Structure, Tertiary
  • Protein Folding
  • Mutation
  • Lasers
  • Hot Temperature
  • Amino Acid Substitution