Molecular-Scale Force Measurement in a Coiled-Coil Peptide Dimer by Electron Spin Resonance

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 α-helical coiled-coil leucine zipper of yeast transcriptional activator GCN4. The equilibrium distribution of distanc...

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Veröffentlicht in:	Journal of the American Chemical Society 2009-04, Vol.131 (15), p.5374-5375
Hauptverfasser:	Gullà, Stefano V, Sharma, Gaurav, Borbat, Peter, Freed, Jack H, Ghimire, Harishchandra, Benedikt, Monica R, Holt, Natasha L, Lorigan, Gary A, Rege, Kaushal, Mavroidis, Constantinos, Budil, David E
Format:	Artikel
Sprache:	eng
Schlagworte:	Basic-Leucine Zipper Transcription Factors - chemistry Chemical Phenomena Electron Spin Resonance Spectroscopy - instrumentation Electron Spin Resonance Spectroscopy - methods Leucine Zippers Methods Peptides - chemistry Protein Multimerization Protein Structure, Secondary Saccharomyces cerevisiae Proteins - chemistry Spin Labels
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Zusammenfassung:	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 α-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.
ISSN:	0002-7863 1520-5126
DOI:	10.1021/ja900230w