ArticleBiophysical journal2001
Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed.
- Correlation between chemical denaturation and the unfolding energetics of Acanthamoeba actophorin.Biophysical journal · 2023Article
- Implementation of Telescoping Boxes in Adaptive Steered Molecular Dynamics.Journal of chemical theory and computation · 2022Article
- Assessing models of force-dependent unbinding rates via infrequent metadynamics.The Journal of chemical physics · 2022Article
- Molten globule-like transition state of protein barnase measured with calorimetric force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein folding mechanism revealed by single-molecule force spectroscopy experiments.Biophysics reports · 2021Article
- Understanding the Thermal Denaturation of Myoglobin with IMS-MS: Evidence for Multiple Stable Structures and Trapped Pre-equilibrium States.Journal of the American Society for Mass Spectrometry · 2021Article
- Influence of Fluorination on Single-Molecule Unfolding and Rupture Pathways of a Mechanostable Protein Adhesion Complex.Nano letters · 2020Article
- Entropic bonding of the type 1 pilus from experiment and simulation.Royal Society open science · 2020Article
- Single-molecule nanopore enzymology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Mechanical Folding and Unfolding of Protein Barnase at the Single-Molecule Level.Biophysical journal · 2016Article
- Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Biochemistry · 2014Article
- Single-molecule studies on PolySUMO proteins reveal their mechanical flexibility.Biophysical journal · 2013Article
- Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Direct observation of proteolytic cleavage at the S2 site upon forced unfolding of the Notch negative regulatory region.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Engineered bi-histidine metal chelation sites map the structure of the mechanical unfolding transition state of an elastomeric protein domain GB1.Biophysical journal · 2012Article
- Tracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter.Biophysical journal · 2012Article
- Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation.Biophysical journal · 2012Article
- Unequivocal single-molecule force spectroscopy of proteins by AFM using pFS vectors.Biophysical journal · 2012Article
- Protein unfolding under force: crack propagation in a network.Biophysical journal · 2011Article
- Molecular basis for the structural stability of an enclosed β-barrel loop.Journal of molecular biology · 2010Article
9 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
Atomic force microscopy (AFM) experiments have provided intriguing insights into the mechanical unfolding of proteins such as titin I27 from muscle, but will the same be possible for proteins that are not physiologically required to resist force? We report the results of AFM experiments on the forced unfolding of barnase in a chimeric construct with I27. Both modules are independently folded and stable in this construct and have the same thermodynamic and kinetic properties as the isolated proteins. I27 can be identified in the AFM traces based on its previous characterization, and distinct, irregular low-force peaks are observed for barnase. Molecular dynamics simulations of barnase unfolding also show that it unfolds at lower forces than proteins with mechanical function. The unfolding pathway involves the unraveling of the protein from the termini, with much more native-like secondary and tertiary structure being retained in the transition state than is observed in simulations of thermal unfolding or experimentally, using chemical denaturant. Our results suggest that proteins that are not selected for tensile strength may not resist force in the same way as those that are, and that proteins with similar unfolding rates in solution need not have comparable unfolding properties under force.
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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.