ArticleBiophysical journal2008
Toward a molecular understanding of the anisotropic response of proteins to external forces: insights from elastic network models.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed.
- Protein Surface Site Determines the Evolutionary Accessibility of Allosteric Regulation.bioRxiv : the preprint server for biology · 2026Article
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- Design of inhibitors to Klebsiella pneumoniae aspartate semialdehyde dehydrogenase towards hospital-acquired infections.Molecular diversity · 2026Article
- Evaluating the ability of in silico identified hit compounds to bind Staphylococcus aureus LcpAMolecular diversity · 2026Article
- High-Throughput Computation of Anharmonic Low-Frequency Protein Vibrations.The journal of physical chemistry. B · 2025Article
- Exploring the unfolding pathways of protein families using Elastic Network Model.Scientific reports · 2024Article
- Structural Dynamics Predominantly Determine the Adaptability of Proteins to Amino Acid Deletions.International journal of molecular sciences · 2023Article
- Cooperative mechanics of PR65 scaffold underlies the allosteric regulation of the phosphatase PP2A.Structure (London, England : 1993) · 2023Article
- Energy Transport alongMaterials (Basel, Switzerland) · 2022Article
- Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.Nanomaterials (Basel, Switzerland) · 2021Article
- Low-Frequency Harmonic Perturbations Drive Protein Conformational Changes.International journal of molecular sciences · 2021Article
- Structural Communication between theInternational journal of molecular sciences · 2021Article
- Structural compliance: A new metric for protein flexibility.Proteins · 2020Article
- Shape-preserving elastic solid models of macromolecules.PLoS computational biology · 2020Article
- Modulation of Toroidal Proteins Dynamics in Favor of Functional Mechanisms upon Ligand Binding.Biophysical journal · 2020Article
- Complementary computational and experimental evaluation of missense variants in the ROMK potassium channel.PLoS computational biology · 2020Article
- Probing the Structural Dynamics of theFrontiers in molecular biosciences · 2020Article
- Characterization of Differential Dynamics, Specificity, and Allostery of Lipoxygenase Family Members.Journal of chemical information and modeling · 2019Article
- Biophysical Characterization Platform Informs Protein Scaffold Evolvability.ACS combinatorial science · 2019Article
- Coarse-Grained Protein Dynamics Studies Using Elastic Network Models.International journal of molecular sciences · 2018Review
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2 authors.
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Abstract
With recent advances in single-molecule manipulation techniques, it is now possible to measure the mechanical resistance of proteins to external pulling forces applied at specific positions. Remarkably, such recent studies demonstrated that the pulling/stretching forces required to initiate unfolding vary considerably depending on the location of the application of the forces, unraveling residue/position-specific response of proteins to uniaxial tension. Here we show that coarse-grained elastic network models based on the topology of interresidue contacts in the native state can satisfactory explain the relative sizes of such stretching forces exerted on different residue pairs. Despite their simplicity, such models presumably capture a fundamental property that dominates the observed behavior: deformations that can be accommodated by the relatively lower frequency modes of motions intrinsically favored by the structure require weaker forces and vice versa. The mechanical response of proteins to external stress is therefore shown to correlate with the anisotropic fluctuation dynamics intrinsically accessible in the folded state. The dependence on the overall fold implies that evolutionarily related proteins sharing common structural features tend to possess similar mechanical properties. However, the theory cannot explain the differences observed in a number of structurally similar but sequentially distant domains, such as the fibronectin domains.
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