ArticlePLoS computational biology2010
Nonlinearity of mechanochemical motions in motor proteins.
Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Simple mechanics of protein machines.Journal of the Royal Society, Interface · 2019Article
- Coarse-Grained Protein Dynamics Studies Using Elastic Network Models.International journal of molecular sciences · 2018Review
- Designed Elastic Networks: Models of Complex Protein Machinery.International journal of molecular sciences · 2018Review
- Deciphering Intrinsic Inter-subunit Couplings that Lead to Sequential Hydrolysis of FBiophysical journal · 2017Article
- Design of Elastic Networks with Evolutionary Optimized Long-Range Communication as Mechanical Models of Allosteric Proteins.Biophysical journal · 2017Article
- Article
- Myosin-V as a mechanical sensor: an elastic network study.Biophysical journal · 2012Article
- Article
- In silico investigation of conformational motions in superfamily 2 helicase proteins.PloS one · 2011Article
- Tracing entire operation cycles of molecular motor hepatitis C virus helicase in structurally resolved dynamical simulations.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Mechanism of processive movement of monomeric and dimeric kinesin molecules.International journal of biological sciences · 2010Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assumption of linear response of protein molecules to thermal noise or structural perturbations, such as ligand binding or detachment, is broadly used in the studies of protein dynamics. Conformational motions in proteins are traditionally analyzed in terms of normal modes and experimental data on thermal fluctuations in such macromolecules is also usually interpreted in terms of the excitation of normal modes. We have chosen two important protein motors--myosin V and kinesin KIF1A--and performed numerical investigations of their conformational relaxation properties within the coarse-grained elastic network approximation. We have found that the linearity assumption is deficient for ligand-induced conformational motions and can even be violated for characteristic thermal fluctuations. The deficiency is particularly pronounced in KIF1A where the normal mode description fails completely in describing functional mechanochemical motions. These results indicate that important assumptions of the theory of protein dynamics may need to be reconsidered. Neither a single normal mode nor a superposition of such modes yields an approximation of strongly nonlinear dynamics.
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