ArticleProceedings of the National Academy of Sciences of the United States of America2012
Rate limit of protein elastic response is tether dependent.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 67 citations in OpenAlex.
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- Effects of Proline on Internal Friction in Simulated Folding Dynamics of Several Alanine-Based α-Helical Peptides.The journal of physical chemistry. B · 2024Article
- Analytical Approaches for Deriving Friction Coefficients for Selected α-Helical Peptides Based Entirely on Molecular Dynamics Simulations.The journal of physical chemistry. B · 2022Article
- Quantitative Elasticity of Flexible Polymer Chains Using Interferometer-Based AFM.Nanomaterials (Basel, Switzerland) · 2022Article
- Nonexponential kinetics captured in sequential unfolding of polyproteins over a range of loads.Current research in structural biology · 2022Article
- Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.Nano letters · 2021Article
- Modulation of a protein-folding landscape revealed by AFM-based force spectroscopy notwithstanding instrumental limitations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Interplay between Viscoelasticity and Force Rate Affects Sequential Unfolding in Polyproteins Pulled at Constant Velocity.Macromolecules · 2020Article
- Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates.Communications biology · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Instrumental Effects in the Dynamics of an Ultrafast Folding Protein under Mechanical Force.The journal of physical chemistry. B · 2018Article
- Probing Position-Dependent Diffusion in Folding Reactions Using Single-Molecule Force Spectroscopy.Biophysical journal · 2018Article
- The Work of Titin Protein Folding as a Major Driver in Muscle Contraction.Annual review of physiology · 2018Review
- Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017Article
- A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics.Journal of the American Chemical Society · 2016Article
- Extracting intrinsic dynamic parameters of biomolecular folding from single-molecule force spectroscopy experiments.Protein science : a publication of the Protein Society · 2016Article
- On artifacts in single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The elastic free energy of a tandem modular protein under force.Biochemical and biophysical research communications · 2015Article
- Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces.Journal of the American Chemical Society · 2015Article
- Determining intrachain diffusion coefficients for biopolymer dynamics from single-molecule force spectroscopy measurements.Biophysical journal · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The elastic restoring force of tissues must be able to operate over the very wide range of loading rates experienced by living organisms. It is surprising that even the fastest events involving animal muscle tissues do not surpass a few hundred hertz. We propose that this limit is set in part by the elastic dynamics of tethered proteins extending and relaxing under a changing load. Here we study the elastic dynamics of tethered proteins using a fast force spectrometer with sub-millisecond time resolution, combined with Brownian and Molecular Dynamics simulations. We show that the act of tethering a polypeptide to an object, an inseparable part of protein elasticity in vivo and in experimental setups, greatly reduces the attempt frequency with which the protein samples its free energy. Indeed, our data shows that a tethered polypeptide can traverse its free-energy landscape with a surprisingly low effective diffusion coefficient D(eff) ~ 1,200 nm(2)/s. By contrast, our Molecular Dynamics simulations show that diffusion of an isolated protein under force occurs at D(eff) ~ 10(8) nm(2)/s. This discrepancy is attributed to the drag force caused by the tethering object. From the physiological time scales of tissue elasticity, we calculate that tethered elastic proteins equilibrate in vivo with D(eff) ~ 10(4)-10(6) nm(2)/s which is two to four orders magnitude smaller than the values measured for untethered proteins in bulk.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.