ArticleProceedings of the National Academy of Sciences of the United States of America2006
Effects of surface tethering on protein folding mechanisms.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
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- The effect of charged residue substitutions on the thermodynamics of protein-surface interactions.Protein science : a publication of the Protein Society · 2021Article
- ABEL-FRET: tether-free single-molecule FRET with hydrodynamic profiling.Nature methods · 2021Article
- Stretching DNA to twice the normal length with single-molecule hydrodynamic trapping.Lab on a chip · 2020Article
- Understanding biochemical processes in the presence of sub-diffusive behavior of biomolecules in solution and living cells.Biophysical reviews · 2019Review
- Interferometric Scattering Enables Fluorescence-Free Electrokinetic Trapping of Single Nanoparticles in Free Solution.Nano letters · 2019Article
- Surface Attachment Enhances the Thermodynamic Stability of Protein L.Angewandte Chemie (International ed. in English) · 2019Article
- Time-resolved multirotational dynamics of single solution-phase tau proteins reveals details of conformational variation.Physical chemistry chemical physics : PCCP · 2019Article
- Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.Angewandte Chemie (International ed. in English) · 2017Article
- The effects of tether placement on antibody stability on surfaces.The Journal of chemical physics · 2017Article
- Novel roles for well-known players: from tobacco mosaic virus pests to enzymatically active assemblies.Beilstein journal of nanotechnology · 2016Review
- In vivo dynamics of skeletal muscle Dystrophin in zebrafish embryos revealed by improved FRAP analysis.eLife · 2015Article
- Single-molecule spectroscopy and imaging over the decades.Faraday discussions · 2015Review
- Single-molecule spectroscopy reveals photosynthetic LH2 complexes switch between emissive states.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- 3Drefine: consistent protein structure refinement by optimizing hydrogen bonding network and atomic-level energy minimization.Proteins · 2013Article
- Probing single biomolecules in solution using the anti-Brownian electrokinetic (ABEL) trap.Accounts of chemical research · 2012Article
- Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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3 authors.
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Abstract
The folding mechanisms of proteins are increasingly being probed through single-molecule experiments in which the protein is immobilized on a surface. Nevertheless, a clear understanding of how the surface might affect folding, and whether or not it changes folding from its bulk behavior, is lacking. In this work, we use molecular dynamics simulations of a model beta-barrel protein tethered to a surface to systematically investigate how the surface impacts folding. In the bulk, this protein folds in a three-state manner through a compact intermediate state, and its transition state (TS) has a well formed hydrophobic core. Upon tethering, we find that folding rates and stability are impacted differently by the surface, with dependencies on both the length and location of the tether. Significant changes in folding times are observed for tether points that do not alter the folding temperature. Tethering also locally enhances the formation of structure for residues proximal to the tether point. We find that neither the folding mechanism nor the TS of this protein are altered if the tether is in a fully structured or completely unstructured region of the TS. By contrast, tethering in a partially structured region of the TS leads to dramatic changes. For one such tether point, the intermediate present in bulk folding is eliminated, leading to a two-state folding process with a heterogeneous, highly unstructured TS ensemble. These results have implications for both the design of single-molecule experiments and biotechnological applications of tethered proteins.
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