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Methionine oxidation of monomeric lambda repressor: the denatured state ensemble under nondenaturing conditions.

Publication ,  Journal Article
Chugha, P; Sage, HJ; Oas, TG
Published in: Protein Sci
March 2006

Although poorly understood, the properties of the denatured state ensemble are critical to the thermodynamics and the kinetics of protein folding. The most relevant conformations to cellular protein folding are the ones populated under physiological conditions. To avoid the problem of low expression that is seen with unstable variants, we used methionine oxidation to destabilize monomeric lambda repressor and predominantly populate the denatured state under nondenaturing buffer conditions. The denatured ensemble populated under these conditions comprises conformations that are compact. Analytical ultracentrifugation sedimentation velocity experiments indicate a small increase in Stokes radius over that of the native state. A significant degree of alpha-helical structure in these conformations is detected by far-UV circular dichroism, and some tertiary interactions are suggested by near-UV circular dichroism. The characteristics of the denatured state populated by methionine oxidation in nondenaturing buffer are very different from those found in chemical denaturant.

Duke Scholars

Published In

Protein Sci

DOI

ISSN

0961-8368

Publication Date

March 2006

Volume

15

Issue

3

Start / End Page

533 / 542

Location

United States

Related Subject Headings

  • Viral Regulatory and Accessory Proteins
  • Viral Proteins
  • Repressor Proteins
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Denaturation
  • Oxidation-Reduction
  • Nuclear Magnetic Resonance, Biomolecular
  • Models, Molecular
 

Citation

APA
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ICMJE
MLA
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Chugha, P., Sage, H. J., & Oas, T. G. (2006). Methionine oxidation of monomeric lambda repressor: the denatured state ensemble under nondenaturing conditions. Protein Sci, 15(3), 533–542. https://doi.org/10.1110/ps.051856406
Chugha, Preeti, Harvey J. Sage, and Terrence G. Oas. “Methionine oxidation of monomeric lambda repressor: the denatured state ensemble under nondenaturing conditions.Protein Sci 15, no. 3 (March 2006): 533–42. https://doi.org/10.1110/ps.051856406.
Chugha, Preeti, et al. “Methionine oxidation of monomeric lambda repressor: the denatured state ensemble under nondenaturing conditions.Protein Sci, vol. 15, no. 3, Mar. 2006, pp. 533–42. Pubmed, doi:10.1110/ps.051856406.

Published In

Protein Sci

DOI

ISSN

0961-8368

Publication Date

March 2006

Volume

15

Issue

3

Start / End Page

533 / 542

Location

United States

Related Subject Headings

  • Viral Regulatory and Accessory Proteins
  • Viral Proteins
  • Repressor Proteins
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Denaturation
  • Oxidation-Reduction
  • Nuclear Magnetic Resonance, Biomolecular
  • Models, Molecular