Long-range energy transfer in proteins
Open accessAbstract
Proteins are large and complex molecular machines. In order to perform their function, most of them need energy, e.g. either in the form of a photon, as in the case of the visual pigment rhodopsin, or through the breaking of a chemical bond, as in the presence of adenosine triphosphate (ATP). Such energy, in turn, has to be transmitted to specific locations, often several tens of A away from where it is initially released. Here we show, within the framework of a coarse-grained nonlinear network model, that energy in a protein can jump from site to site with high yields, covering in many instances remarkably large distances. Following single-site excitations, few specific sites are targeted, systematically within the stiffest regions. Such energy transfers mark the spontaneous formation of a localized mode of nonlinear origin at the destination site, which acts as an efficient energy-accumulating center. Interestingly, yields are found to be optimum for excitation energies in the range of biologically relevant ones.
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Propagation of conformational change at certain locations can cause large-amplitude fluctuations of linked domains.
“The propagation of conformational change at certain locations228–230 can lead to large amplitude fluctuations of the linked domains.231”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [230]
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- Authors
- Piazza, F., & Sanejouand, Y.-H.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Centre National de la Recherche Scientifique (FR)
- Venue
- Physical Biology
- Publisher
- IOP Publishing
- Published
- 2009-11-12
- Volume
- 6
- Issue
- 4
- Pages
- 046014
- ISSN
- 1478-3967 (ISSN-L)
- 1478-3975
- OpenAlex
- W1994621063
- Cited by
- 58
- References
- 67
- Citations by year
- 2025: 1 · 2020: 2 · 2019: 2 · 2017: 3 · 2016: 7 · 2015: 3 · 2014: 11 · 2013: 7 · 2012: 8
- FWCI
- 4.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Physical Biology (publishedVersion)
- PubMed (publishedVersion)
- arXiv (Cornell University) (submittedVersion)
- HAL (submittedVersion)
- Florence Research (University of Florence) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- arXiv (Cornell University)
- Topics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- long-range energy transfer, proteins, nonlinear network model, coarse-grained models, rhodopsin, ATP, energy accumulation, localized modes, excitation energies, protein dynamics
- MeSH terms
- Energy Transfer, Models, Biological, Proteins, Nonlinear Dynamics
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