ArticleProceedings of the National Academy of Sciences of the United States of America2007
Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- An optical aptasensor for real-time quantification of endotoxin: From ensemble to single-molecule resolution.Science advances · 2023Article
- Protein chain collapse modulation and folding stimulation by GroEL-ES.Science advances · 2022Article
- Quantitative Elasticity of Flexible Polymer Chains Using Interferometer-Based AFM.Nanomaterials (Basel, Switzerland) · 2022Article
- Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022Article
- Entropy-Enthalpy Compensations Fold Proteins in Precise Ways.International journal of molecular sciences · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.Nano letters · 2021Article
- Thermal inactivation scaling applied for SARS-CoV-2.Biophysical journal · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Structural Origins of FRET-Observed Nascent Chain Compaction on the Ribosome.The journal of physical chemistry. B · 2018Article
- The force-dependent mechanism of DnaK-mediated mechanical folding.Science advances · 2018Article
- Proteins Breaking Bad: A Free Energy Perspective.The journal of physical chemistry letters · 2017Article
- Can Co-Activation of Nrf2 and Neurotrophic Signaling Pathway Slow Alzheimer's Disease?International journal of molecular sciences · 2017Review
- Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding.Nature communications · 2016Article
- How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Elasticity, structure, and relaxation of extended proteins under force.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.Nature protocols · 2013Article
- Conformational dynamics of titin PEVK explored with FRET spectroscopy.Biophysical journal · 2012Article
- Rate limit of protein elastic response is tether dependent.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Direct quantification of the attempt frequency determining the mechanical unfolding of ubiquitin protein.The Journal of biological chemistry · 2011Article
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Authors and funding
6 authors.
Funding
Abstract
We unfold and extend single proteins at a high force and then linearly relax the force to probe their collapse mechanisms. We observe a large variability in the extent of their recoil. Although chain entropy makes a small contribution, we show that the observed variability results from hydrophobic interactions with randomly varying magnitude from protein to protein. This collapse mechanism is common to highly extended proteins, including nonfolding elastomeric proteins like PEVK from titin. Our observations explain the puzzling differences between the folding behavior of highly extended proteins, from those folding after chemical or thermal denaturation. Probing the collapse of highly extended proteins with force spectroscopy allows separation of the different driving forces in protein folding.
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