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Submillisecond folding of monomeric lambda repressor.

Publication ,  Journal Article
Huang, GS; Oas, TG
Published in: Proc Natl Acad Sci U S A
July 18, 1995

The folding kinetics of a truncated form of the N-terminal domain of phage lambda repressor [lambda 6-85] has been investigated by using the technique of dynamic NMR. lambda 6-85 has been shown previously to fold in a purely two-state fashion. This allows the determination of folding and unfolding rates from simulation of the exchange-broadened aromatic resonances of Tyr-22. The folding kinetics were determined over a range of 1.35 to 3.14 M urea. The urea dependence of both folding and unfolding rate constants is exponential, suggesting that the rate-determining step is invariant at the urea concentrations studied. The folding and unfolding rates extrapolated to 0 M urea at 37 degrees C are 3600 +/- 400 s-1 and 27 +/- 6 s-1, respectively. The observed lambda 6-85 folding rate constant exceeds that of other fast-folding globular proteins by a factor of 14-54. The urea dependence of the folding and unfolding rate constants suggests that the transition state of the rate-determining step is considerably more exposed to solvent than previously studied protein-folding transition states. The surprising rapidity of lambda 6-85 folding and unfolding may be the consequence of its all-helical secondary structure. These kinetic results clearly demonstrate that all of the fundamental events of protein folding can occur on the submillisecond time scale.

Duke Scholars

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

July 18, 1995

Volume

92

Issue

15

Start / End Page

6878 / 6882

Location

United States

Related Subject Headings

  • Viral Regulatory and Accessory Proteins
  • Viral Proteins
  • Urea
  • Time Factors
  • Repressor Proteins
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Denaturation
  • Peptide Fragments
  • Models, Molecular
 

Citation

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MLA
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Huang, G. S., & Oas, T. G. (1995). Submillisecond folding of monomeric lambda repressor. Proc Natl Acad Sci U S A, 92(15), 6878–6882. https://doi.org/10.1073/pnas.92.15.6878
Huang, G. S., and T. G. Oas. “Submillisecond folding of monomeric lambda repressor.Proc Natl Acad Sci U S A 92, no. 15 (July 18, 1995): 6878–82. https://doi.org/10.1073/pnas.92.15.6878.
Huang GS, Oas TG. Submillisecond folding of monomeric lambda repressor. Proc Natl Acad Sci U S A. 1995 Jul 18;92(15):6878–82.
Huang, G. S., and T. G. Oas. “Submillisecond folding of monomeric lambda repressor.Proc Natl Acad Sci U S A, vol. 92, no. 15, July 1995, pp. 6878–82. Pubmed, doi:10.1073/pnas.92.15.6878.
Huang GS, Oas TG. Submillisecond folding of monomeric lambda repressor. Proc Natl Acad Sci U S A. 1995 Jul 18;92(15):6878–6882.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

July 18, 1995

Volume

92

Issue

15

Start / End Page

6878 / 6882

Location

United States

Related Subject Headings

  • Viral Regulatory and Accessory Proteins
  • Viral Proteins
  • Urea
  • Time Factors
  • Repressor Proteins
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Denaturation
  • Peptide Fragments
  • Models, Molecular