Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin

Jasna Brujić; Rodolfo I.Z. Hermans; Kirstin A. Walther; Julio M. Fernandez

doi:10.1038/nphys269

Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin

Jasna Brujić, Rodolfo I.Z. Hermans, Kirstin A. Walther, Julio M. Fernandez

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Abstract

The conformational energy landscape of a protein out of equilibrium is poorly understood. We use single-molecule force-clamp spectroscopy to measure the kinetics of unfolding of the protein ubiquitin under a constant force. We discover a surprisingly broad distribution of unfolding rates that follows a power law with no characteristic mean. The structural fluctuations that give rise to this distribution reveal the architecture of the protein's energy landscape. Following models of glassy dynamics, this complex kinetics implies large fluctuations in the energies of the folded protein, characterized by an exponential distribution with a width of 5-10kBT. Our results predict the existence of a 'glass transition' force below which the folded conformations interconvert between local minima on multiple timescales. These techniques offer a new tool to further test statistical energy landscape theories experimentally.

Original language	English (US)
Pages (from-to)	282-286
Number of pages	5
Journal	Nature Physics
Volume	2
Issue number	4
DOIs	https://doi.org/10.1038/nphys269
State	Published - Apr 2006

ASJC Scopus subject areas

General Physics and Astronomy

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title = "Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin",

abstract = "The conformational energy landscape of a protein out of equilibrium is poorly understood. We use single-molecule force-clamp spectroscopy to measure the kinetics of unfolding of the protein ubiquitin under a constant force. We discover a surprisingly broad distribution of unfolding rates that follows a power law with no characteristic mean. The structural fluctuations that give rise to this distribution reveal the architecture of the protein's energy landscape. Following models of glassy dynamics, this complex kinetics implies large fluctuations in the energies of the folded protein, characterized by an exponential distribution with a width of 5-10kBT. Our results predict the existence of a 'glass transition' force below which the folded conformations interconvert between local minima on multiple timescales. These techniques offer a new tool to further test statistical energy landscape theories experimentally.",

author = "Jasna Bruji{\'c} and Hermans, {Rodolfo I.Z.} and Walther, {Kirstin A.} and Fernandez, {Julio M.}",

note = "Funding Information: We would like to thank H. H. Huang for making the ubiquitin construct, S. Garcia-Manyes for data collection, and H. A. Makse and A. J. Tolley for enlightening discussions. This work has been supported by NIH grant R01 HL66030 to J.M.F. Correspondence and requests for materials should be addressed to J.B. or J.M.F. Supplementary Information accompanies this paper on www.nature.com/naturephysics. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.",

year = "2006",

month = apr,

doi = "10.1038/nphys269",

language = "English (US)",

volume = "2",

pages = "282--286",

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AU - Brujić, Jasna

AU - Hermans, Rodolfo I.Z.

AU - Walther, Kirstin A.

AU - Fernandez, Julio M.

N1 - Funding Information: We would like to thank H. H. Huang for making the ubiquitin construct, S. Garcia-Manyes for data collection, and H. A. Makse and A. J. Tolley for enlightening discussions. This work has been supported by NIH grant R01 HL66030 to J.M.F. Correspondence and requests for materials should be addressed to J.B. or J.M.F. Supplementary Information accompanies this paper on www.nature.com/naturephysics. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.

PY - 2006/4

Y1 - 2006/4

N2 - The conformational energy landscape of a protein out of equilibrium is poorly understood. We use single-molecule force-clamp spectroscopy to measure the kinetics of unfolding of the protein ubiquitin under a constant force. We discover a surprisingly broad distribution of unfolding rates that follows a power law with no characteristic mean. The structural fluctuations that give rise to this distribution reveal the architecture of the protein's energy landscape. Following models of glassy dynamics, this complex kinetics implies large fluctuations in the energies of the folded protein, characterized by an exponential distribution with a width of 5-10kBT. Our results predict the existence of a 'glass transition' force below which the folded conformations interconvert between local minima on multiple timescales. These techniques offer a new tool to further test statistical energy landscape theories experimentally.

AB - The conformational energy landscape of a protein out of equilibrium is poorly understood. We use single-molecule force-clamp spectroscopy to measure the kinetics of unfolding of the protein ubiquitin under a constant force. We discover a surprisingly broad distribution of unfolding rates that follows a power law with no characteristic mean. The structural fluctuations that give rise to this distribution reveal the architecture of the protein's energy landscape. Following models of glassy dynamics, this complex kinetics implies large fluctuations in the energies of the folded protein, characterized by an exponential distribution with a width of 5-10kBT. Our results predict the existence of a 'glass transition' force below which the folded conformations interconvert between local minima on multiple timescales. These techniques offer a new tool to further test statistical energy landscape theories experimentally.

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Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin

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