The Energy Landscapes and Motions of Proteins
Abstract
Recent experiments, advances in theory, and analogies to other complex systems such as glasses and spin glasses yield insight into protein dynamics. The basis of the understanding is the observation that the energy landscape is complex: Proteins can assume a large number of nearly isoenergetic conformations (conformational substates). The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.
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All soluble proteins exist as conformational ensembles in equilibrium around their native states.
“In the cell, the conformational ensembles of all soluble proteins are in equilibrium around their native states.1”
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 [1]
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- Authors
- Frauenfelder, H., Sligar, S. G., & Wolynes, P. G.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Venue
- Science
- Published
- 1991-12-13
- Volume
- 254
- Issue
- 5038
- Pages
- 1598-1603
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2094795801
- Cited by
- 3,250
- References
- 85
- Citations by year
- 2026: 116 · 2025: 94 · 2024: 85 · 2023: 91 · 2022: 133 · 2021: 122 · 2020: 104 · 2019: 103 · 2018: 88 · 2017: 101 · 2016: 122 · 2015: 118 · 2014: 122 · 2013: 157 · 2012: 126
- FWCI
- 12.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Diffusion and Search Dynamics
- Keywords
- protein energy landscape, protein dynamics, conformational substates, conformational isomerism, protein folding, protein-ligand binding, myoglobin, carbon monoxide binding, spin glass, glass
- MeSH terms
- Carbon Monoxide, Chemistry, Physical, Motion, Myoglobin, Protein Conformation, Structure-Activity Relationship, Temperature, Thermodynamics, Chemical Phenomena
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