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

doi:10.1021/ja900230w

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

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

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 language	English (US)
Pages (from-to)	5374-5375
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	131
Issue number	15
DOIs	https://doi.org/10.1021/ja900230w
State	Published - Apr 22 2009

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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title = "Molecular-scale force measurement in a coiled-coil peptide dimer by electron spin resonance",

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.",

author = "Gull{\`a}, {Stefano V.} and Gaurav Sharma and Peter Borbat and Freed, {Jack H.} and Harishchandra Ghimire and Benedikt, {Monica R.} and Holt, {Natasha L.} and Lorigan, {Gary A.} and Kaushal Rege and Constantinos Mavroidis and Budil, {David E.}",

year = "2009",

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doi = "10.1021/ja900230w",

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T1 - Molecular-scale force measurement in a coiled-coil peptide dimer by electron spin resonance

AU - Gullà, Stefano V.

AU - Sharma, Gaurav

AU - Borbat, Peter

AU - Freed, Jack H.

AU - Ghimire, Harishchandra

AU - Benedikt, Monica R.

AU - Holt, Natasha L.

AU - Lorigan, Gary A.

AU - Rege, Kaushal

AU - Mavroidis, Constantinos

AU - Budil, David E.

PY - 2009/4/22

Y1 - 2009/4/22

N2 - 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.

AB - 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.

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DO - 10.1021/ja900230w

M3 - Article

C2 - 19331323

AN - SCOPUS:67749118154

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SP - 5374

EP - 5375

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 15

ER -

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

Abstract

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