ArticleProceedings of the National Academy of Sciences of the United States of America2013
Elasticity, structure, and relaxation of extended proteins under force.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
42 citing papers in PubMed.
- Structure-informed theoretical modeling defines principles governing avidity in bivalent protein interactions.The Journal of biological chemistry · 2026Article
- Fine structural tuning of the assembly of elastin-collagen peptide conjugates with drug loading and manipulation of molecular interactions.Biomaterials science · 2026Article
- Influence of Charge Block Length on Conformation and Cluster Formation of Atactic Peptide Polyampholytes.Macromolecules · 2026Article
- Static and dynamic rough energy landscapes can lead to identical diffusivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Intramolecular loops control SARS-CoV-2 nucleocapsid protein self-association and nucleic acid binding dependent on phosphorylation.bioRxiv : the preprint server for biology · 2026Article
- Hidden route of protein damage through oxygen-confined photooxidation.Nature communications · 2024Article
- Blobs form during the single-file transport of proteins across nanopores.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanistic Insight into the Mechanical Unfolding of the Integral Membrane Diacylglycerol Kinase.JACS Au · 2024Article
- Improved Prediction of Molecular Response to Pulling by Combining Force Tempering with Replica Exchange Methods.The journal of physical chemistry. B · 2024Article
- Article
- An optical aptasensor for real-time quantification of endotoxin: From ensemble to single-molecule resolution.Science advances · 2023Article
- Effects of Sequence Composition, Patterning and Hydrodynamics on the Conformation and Dynamics of Intrinsically Disordered Proteins.International journal of molecular sciences · 2023Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- The stoichiometric interaction model for mesoscopic MD simulations of liquid-liquid phase separation.Biophysical journal · 2022Article
- Single-molecule investigations of single-chain cellulose biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Assessing models of force-dependent unbinding rates via infrequent metadynamics.The Journal of chemical physics · 2022Article
- Molecular Paradigms for Biological Mechanosensing.The journal of physical chemistry. B · 2021Article
- Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.Nano letters · 2021Article
- Fine structural tuning of the assembly of ECM peptide conjugates via slight sequence modifications.Science advances · 2020Article
- Article
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Authors and funding
4 authors.
Funding
Abstract
Force spectroscopies have emerged as a powerful and unprecedented tool to study and manipulate biomolecules directly at a molecular level. Usually, protein and DNA behavior under force is described within the framework of the worm-like chain (WLC) model for polymer elasticity. Although it has been surprisingly successful for the interpretation of experimental data, especially at high forces, the WLC model lacks structural and dynamical molecular details associated with protein relaxation under force that are key to the understanding of how force affects protein flexibility and reactivity. We use molecular dynamics simulations of ubiquitin to provide a deeper understanding of protein relaxation under force. We find that the WLC model successfully describes the simulations of ubiquitin, especially at higher forces, and we show how protein flexibility and persistence length, probed in the force regime of the experiments, are related to how specific classes of backbone dihedral angles respond to applied force. Although the WLC model is an average, backbone model, we show how the protein side chains affect the persistence length. Finally, we find that the diffusion coefficient of the protein's end-to-end distance is on the order of 10(8) nm(2)/s, is position and side-chain dependent, but is independent of the length and independent of the applied force, in contrast with other descriptions.
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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.