Molecular-scale force measurement in a coiled-coil peptide dimer by electron spin resonance

Stefano V. Gullà, Gaurav Sharma, Peter Borbat, Jack H. Freed, Harishchandra Ghimire, Monica R. Benedikt, Natasha L. Holt, Gary A. Lorigan, Kaushal Rege, Constantinos Mavroidis, David E. Budil

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Abstract

A new method for measuring forces between small protein domains based on double electron-electron resonance (DEER) spectroscopy is demonstrated using a model peptide derived from the C-helical coiled-coil leucine zipper of yeast transcriptional activator GCN4. The equilibrium distribution of distances between two nitroxide spin labels rigidly attached to the helices of the dimer was determined by DEER and yielded a closing force of 100 ± 10 pN between monomers, in excellent agreement with theoretical predictions.

Original languageEnglish (US)
Pages (from-to)5374-5375
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number15
DOIs
StatePublished - Apr 22 2009

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Gullà, S. V., Sharma, G., Borbat, P., Freed, J. H., Ghimire, H., Benedikt, M. R., Holt, N. L., Lorigan, G. A., Rege, K., Mavroidis, C., & Budil, D. E. (2009). Molecular-scale force measurement in a coiled-coil peptide dimer by electron spin resonance. Journal of the American Chemical Society, 131(15), 5374-5375. https://doi.org/10.1021/ja900230w