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Direct Observation of the Three-State Folding of a Single Protein Molecule

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Outgoing claims: the papers this work cites, builds on, or argues with.

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Complete Unfolding of the Titin Molecule under External Force
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Destabilization of the Escherichia coli RNase H Kinetic Intermediate: Switching Between a Two-state and Three-state Folding Mechanism
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The Mechanical Hierarchies of Fibronectin Observed with Single-molecule AFM
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[7] Optical-trap force transducer that operates by direct measurement of light momentum
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The effect of force on thermodynamics and kinetics of single molecule reactions
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Kinetic role of early intermediates in protein folding
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Is protein folding hierarchic? II. Folding intermediates and transition states
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Two-State Folding Observed in Individual Protein Molecules
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Stretching DNA
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Confirmation of the hierarchical folding of RNase H: a protein engineering study.
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The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
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Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
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The mechanical stability of ubiquitin is linkage dependent
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Pulling geometry defines the mechanical resistance of a β-sheet protein
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The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
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Reversible Unfolding of Single RNA Molecules by Mechanical Force
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Force-Clamp Spectroscopy Monitors the Folding Trajectory of a Single Protein
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Folding-Unfolding Transitions in Single Titin Molecules Characterized with Laser Tweezers
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INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS
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Mechanical Processes in Biochemistry

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Collapse Dynamics of Single Proteins Extended by Force
inferred← citeshttps://doi.org/10.1016/j.bpj.2010.12.3700openalex-snapshot
Improved High-Force Magnetic Tweezers for Stretching and Refolding of Proteins and Short DNA
inferred← citeshttps://doi.org/10.1016/j.bpj.2011.02.021openalex-snapshot
Mechanically Unfolding Protein L Using a Laser-Feedback-Controlled Cantilever
inferred← citeshttps://doi.org/10.1016/j.bpj.2011.05.072openalex-snapshot
Protein Unfolding under Force: Crack Propagation in a Network
inferred← citeshttps://doi.org/10.1016/j.bpj.2012.06.051openalex-snapshot
Limitations of Constant-Force-Feedback Experiments
inferred← citeshttps://doi.org/10.1016/j.bpj.2013.08.007openalex-snapshot
Interrogating Biology with Force: Single Molecule High-Resolution Measurements with Optical Tweezers
inferred← citeshttps://doi.org/10.1016/j.bpj.2015.05.028openalex-snapshot
Single-Molecule Folding Mechanisms of the apo- and Mg2+-Bound States of Human Neuronal Calcium Sensor-1
inferred← citeshttps://doi.org/10.1016/j.bpj.2015.11.015openalex-snapshot
Mechanical Folding and Unfolding of Protein Barnase at the Single-Molecule Level
inferred← citeshttps://doi.org/10.1016/j.bpj.2015.12.003openalex-snapshot
Structure-Based Derivation of Protein Folding Intermediates and Energies from Optical Tweezers
inferred← citeshttps://doi.org/10.1016/j.bpj.2015.12.042openalex-snapshot
Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates
inferred← citeshttps://doi.org/10.1016/j.bpj.2016.09.045openalex-snapshot
Hidden Markov Modeling with Detailed Balance and Its Application to Single Protein Folding
inferred← citeshttps://doi.org/10.1016/j.bpj.2017.03.028openalex-snapshot
Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase
inferred← citeshttps://doi.org/10.1016/j.bpj.2017.10.023openalex-snapshot
Force Spectroscopy with 9-μs Resolution and Sub-pN Stability by Tailoring AFM Cantilever Geometry
inferred← citeshttps://doi.org/10.1016/j.bpj.2017.12.038openalex-snapshot
Rare Dissipative Transitions Punctuate the Initiation of Chemical Denaturation in Proteins
inferred← citeshttps://doi.org/10.1016/j.bpj.2019.10.040openalex-snapshot
The Anti-Aggregation Holdase Hsp33 Promotes the Formation of Folded Protein Structures
inferred← citeshttps://doi.org/10.1016/j.bpj.2020.09.016openalex-snapshot
Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein
inferred← citeshttps://doi.org/10.1016/j.bpj.2021.05.003openalex-snapshot
Facile tethering of stable and unstable proteins for optical tweezers experiments
inferred← citeshttps://doi.org/10.1016/j.bpj.2021.09.026openalex-snapshot
Single-molecule optical tweezers reveals folding steps of the domain swapping mechanism of a protein
inferred← citeshttps://doi.org/10.1016/j.bpj.2021.11.2884openalex-snapshot
Single-molecule manipulation of macromolecules on GUV or SUV membranes using optical tweezers
inferred← citeshttps://doi.org/10.1016/j.bpj.2022.11.1030openalex-snapshot
Nonlinear compliance of NOMPC gating spring and its implication in mechanotransduction
inferred← citeshttps://doi.org/10.1016/j.bpj.2026.08.017openalex-snapshot
Single-molecule force spectroscopy reveals a high-force requirement for dissociation of integrin transmembrane domains
inferred← citeshttps://doi.org/10.1016/j.cbpa.2019.09.008openalex-snapshot
Towards biological applications of nanophotonic tweezers
inferred← citeshttps://doi.org/10.1016/j.cell.2011.03.036openalex-snapshot
Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine
inferred← citeshttps://doi.org/10.1016/j.cell.2011.04.010openalex-snapshot
ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates
inferred← citeshttps://doi.org/10.1016/j.cell.2013.09.022openalex-snapshot
The ClpXP Protease Unfolds Substrates Using a Constant Rate of Pulling but Different Gears
inferred← citeshttps://doi.org/10.1016/j.celrep.2016.03.050openalex-snapshot
α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.114110openalex-snapshot
Probing the stability and interdomain interactions in the ABC transporter OpuA using single-molecule optical tweezers
inferred← citeshttps://doi.org/10.1016/j.cels.2021.05.009openalex-snapshot
Fundamentals to function: Quantitative and scalable approaches for measuring protein stability
inferred← citeshttps://doi.org/10.1016/j.chemphys.2011.03.026openalex-snapshot
A combined single-molecule FRET and tryptophan fluorescence study of RNase H folding under acidic conditions
inferred← citeshttps://doi.org/10.1016/j.cplett.2009.05.027openalex-snapshot
Molecular Dynamics insight into the role of tertiary (foldon) interactions on unfolding in Cytochrome c
inferred← citeshttps://doi.org/10.1016/j.crstbi.2021.09.003openalex-snapshot
A hierarchy of coupling free energies underlie the thermodynamic and functional architecture of protein structures
inferred← citeshttps://doi.org/10.1016/j.csbj.2021.08.017openalex-snapshot
Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches
inferred← citeshttps://doi.org/10.1016/j.drudis.2006.05.003openalex-snapshot
Downscaling functional bioassays by single-molecule techniques
inferred← citeshttps://doi.org/10.1016/j.drudis.2022.103443openalex-snapshot
Optical tweezers for drug discovery
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.04.033openalex-snapshot
Ultrastable atomic force microscopy: Improved force and positional stability
inferred← citeshttps://doi.org/10.1016/j.ijleo.2016.01.170openalex-snapshot
Optical gradient force of linearly polarized sine-azimuthal Lorentz beam with one on-axis optical vortex
inferred← citeshttps://doi.org/10.1016/j.ijleo.2016.10.072openalex-snapshot
Tunable optical gradient force of radially polarized Lorentz-Gauss vortex beam by sine-azimuthal variation wavefront
inferred← citeshttps://doi.org/10.1016/j.jbc.2023.105150openalex-snapshot
The adenylate cyclase toxin RTX domain follows a series templated folding mechanism with implications for toxin activity
inferred← citeshttps://doi.org/10.1016/j.jmb.2005.12.061openalex-snapshot
Single-molecule FRET Study of Denaturant Induced Unfolding of RNase H
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.04.035openalex-snapshot
Order of Steps in the Cytochrome c Folding Pathway: Evidence for a Sequential Stabilization Mechanism
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.06.014openalex-snapshot
Single Molecule Force Spectroscopy Reveals a Weakly Populated Microstate of the FnIII Domains of Tenascin
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.10.041openalex-snapshot
Probing Interactions within the Synaptic DNA-SfiI Complex by AFM Force Spectroscopy
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.12.005openalex-snapshot
A Tightly Packed Hydrophobic Cluster Directs the Formation of an Off-pathway Sub-millisecond Folding Intermediate in the α Subunit of Tryptophan Synthase, a TIM Barrel Protein
inferred← citeshttps://doi.org/10.1016/j.jmb.2007.07.071openalex-snapshot
The Rough Energy Landscape of Superfolder GFP Is Linked to the Chromophore
inferred← citeshttps://doi.org/10.1016/j.jmb.2007.11.010openalex-snapshot
NMR Analysis of Partially Folded States and Persistent Structure in the Alpha Subunit of Tryptophan Synthase: Implications for the Equilibrium Folding Mechanism of a 29-kDa TIM Barrel Protein
inferred← citeshttps://doi.org/10.1016/j.jmb.2007.12.020openalex-snapshot
The Foldon Substructure of Staphylococcal Nuclease
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.09.044openalex-snapshot
The High-Resolution NMR Structure of the Early Folding Intermediate of the Thermus thermophilus Ribonuclease H
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.05.084openalex-snapshot
A Single Mutation at Residue 25 Populates the Folding Intermediate of E. coli RNase H and Reveals a Highly Dynamic Partially Folded Ensemble
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.05.085openalex-snapshot
The Folding Trajectory of RNase H Is Dominated by Its Topology and Not Local Stability: A Protein Engineering Study of Variants that Fold via Two-State and Three-State Mechanisms
inferred← citeshttps://doi.org/10.1016/j.jmb.2014.10.003openalex-snapshot
Non-Native Structure Appears in Microseconds during the Folding of E. coli RNase H
inferred← citeshttps://doi.org/10.1016/j.jmb.2015.07.002openalex-snapshot
Gradual Folding of an Off-Pathway Molten Globule Detected at the Single-Molecule Level
inferred← citeshttps://doi.org/10.1016/j.jmb.2016.09.006openalex-snapshot
The Power of Force: Insights into the Protein Folding Process Using Single-Molecule Force Spectroscopy
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.05.021openalex-snapshot
Applications of Single-Molecule Methods to Membrane Protein Folding Studies
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.07.022openalex-snapshot
Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.09.004openalex-snapshot
Protein Folding Mediated by Trigger Factor and Hsp70: New Insights from Single-Molecule Approaches
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.10.012openalex-snapshot
Two Disease-Causing SNAP-25B Mutations Selectively Impair SNARE C-terminal Assembly
inferred← citeshttps://doi.org/10.1016/j.jmb.2021.167126openalex-snapshot
The Protein Folding Problem: The Role of Theory
inferred← citeshttps://doi.org/10.1016/j.jmb.2021.167207openalex-snapshot
Single-Molecule Force Spectroscopy of Protein Folding
inferred← citeshttps://doi.org/10.1016/j.jmb.2021.167325openalex-snapshot
Folding Intermediates, Heterogeneous Native Ensembles and Protein Function
inferred← citeshttps://doi.org/10.1016/j.jmb.2024.168521openalex-snapshot
Anthrax Toxin: Model System for Studying Protein Translocation
inferred← citeshttps://doi.org/10.1016/j.jmgm.2024.108802openalex-snapshot
NPEX: Never give up protein exploration with deep reinforcement learning
inferred← citeshttps://doi.org/10.1016/j.jmr.2022.107196openalex-snapshot
Motional clustering in supra- τ c conformational exchange influences NOE cross-relaxation rate
inferred← citeshttps://doi.org/10.1016/j.jsb.2016.01.009openalex-snapshot
Optimizing force spectroscopy by modifying commercial cantilevers: Improved stability, precision, and temporal resolution
inferred← citeshttps://doi.org/10.1016/j.molcel.2006.10.017openalex-snapshot
Single-Molecule Biology: What Is It and How Does It Work?
inferred← citeshttps://doi.org/10.1016/j.molcel.2019.01.043openalex-snapshot
The Ribosome Cooperates with a Chaperone to Guide Multi-domain Protein Folding
inferred← citeshttps://doi.org/10.1016/j.optcom.2025.132336openalex-snapshot
Tunable autofocusing performance with multi-Airy-Gaussian beams in optical manipulation
inferred← citeshttps://doi.org/10.1016/j.physleta.2018.04.044openalex-snapshot
Dynamic disorder characteristics of single-molecule pulling experiments on two-dimensional free-energy landscape
inferred← citeshttps://doi.org/10.1016/j.physrep.2009.11.001openalex-snapshot
Biomolecules under mechanical force
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