On the public citation graph

Direct Measurement of Barrier Heights in Protein Folding

0 signed · 92 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

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

inferredcites →https://doi.org/10.1002/1097-0134(20000901)40:4<543::aid-prot20>3.0.co;2-oopenalex-snapshot
Modeling protein density of states: Additive hydrophobic effects are insufficient for calorimetric two-state cooperativity
inferredcites →https://doi.org/10.1002/prot.20172openalex-snapshot
The nature of the free energy barriers to two‐state folding
inferredcites →https://doi.org/10.1002/prot.340210302openalex-snapshot
Funnels, pathways, and the energy landscape of protein folding: A synthesis
inferredcites →https://doi.org/10.1007/978-3-642-58760-3openalex-snapshot
Protein Stability and Folding
inferredcites →https://doi.org/10.1016/j.chemphys.2004.06.064openalex-snapshot
Combinatorial modeling of protein folding kinetics: free energy profiles and rates
inferredcites →https://doi.org/10.1016/j.sbi.2004.01.013openalex-snapshot
The protein folding ‘speed limit’
inferredcites →https://doi.org/10.1016/s0076-6879(04)80017-xopenalex-snapshot
Native State Hydrogen-Exchange Analysis of Protein Folding and Protein Motional Domains
inferredcites →https://doi.org/10.1038/nature01060openalex-snapshot
Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
inferredcites →https://doi.org/10.1038/nature01565openalex-snapshot
Erratum: Antibody neutralization and escape by HIV-1
inferredcites →https://doi.org/10.1073/pnas.0405829101openalex-snapshot
Exploring protein-folding ensembles: A variable-barrier model for the analysis of equilibrium unfolding experiments
inferredcites →https://doi.org/10.1073/pnas.92.21.9801openalex-snapshot
Simple model of protein folding kinetics.
inferredcites →https://doi.org/10.1088/0953-8984/17/18/008openalex-snapshot
Diffusional limits to the speed of protein folding: fact or friction?
inferredcites →https://doi.org/10.1146/annurev.physchem.48.1.545openalex-snapshot
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
inferredcites →https://doi.org/10.1385/0896033015openalex-snapshot
Protein Stability and Folding

What points at this work

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

inferred← citeshttps://doi.org/10.2139/ssrn.4841883openalex-extracted
Dierential Scanning Calorimetry of Proteins and Zimm-Bragg Model in Water
inferred← citeshttps://doi.org/10.1002/bip.20537openalex-snapshot
Computational design of proteins stereochemically optimized in size, stability, and folding speed
inferred← citeshttps://doi.org/10.1002/prot.21066openalex-snapshot
Criteria for downhill protein folding: Calorimetry, chevron plot, kinetic relaxation, and single‐molecule radius of gyration in chain models with subdued degrees of cooperativity
inferred← citeshttps://doi.org/10.1002/prot.22001openalex-snapshot
All‐atom replica exchange molecular simulation of protein BBL
inferred← citeshttps://doi.org/10.1007/978-1-0716-1716-8_10openalex-snapshot
NMR Analysis of Protein Folding Interaction Networks
inferred← citeshttps://doi.org/10.1007/978-1-0716-1716-8_5openalex-snapshot
Folding Free Energy Surfaces from Differential Scanning Calorimetry
inferred← citeshttps://doi.org/10.1007/978-1-62703-065-6_13openalex-snapshot
Protein Folding at Atomic Resolution: Analysis of Autonomously Folding Supersecondary Structure Motifs by Nuclear Magnetic Resonance
inferred← citeshttps://doi.org/10.1007/978-981-99-2079-2_3openalex-snapshot
Applications of Differential Scanning Calorimetry in Studying Folding and Stability of Proteins
inferred← citeshttps://doi.org/10.1016/bs.mie.2015.08.027openalex-snapshot
Modern Analysis of Protein Folding by Differential Scanning Calorimetry
inferred← citeshttps://doi.org/10.1016/j.ab.2019.02.008openalex-snapshot
Sarkosyl: A milder detergent than SDS for identifying proteins with moderately high hyperstability using gel electrophoresis
inferred← citeshttps://doi.org/10.1016/j.abb.2024.110132openalex-snapshot
Differential scanning calorimetry of proteins and Zimm–Bragg model in water
inferred← citeshttps://doi.org/10.1016/j.bbapap.2010.09.013openalex-snapshot
Dynamics of protein folding: Probing the kinetic network of folding–unfolding transitions with experiment and theory
inferred← citeshttps://doi.org/10.1016/j.bpc.2010.02.004openalex-snapshot
Protein kinetic stability
inferred← citeshttps://doi.org/10.1016/j.bpj.2018.05.039openalex-snapshot
Dynamics of Dystrophin’s Actin-Binding Domain
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2016.05.006openalex-snapshot
The (unusual) aspartic acid in the metal coordination sphere of the prokaryotic zinc finger domain
inferred← citeshttps://doi.org/10.1016/j.jmb.2006.07.065openalex-snapshot
Natural Selection for Kinetic Stability Is a Likely Origin of Correlations between Mutational Effects on Protein Energetics and Frequencies of Amino Acid Occurrences in Sequence Alignments
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.06.081openalex-snapshot
Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains
inferred← citeshttps://doi.org/10.1016/j.jmb.2010.01.071openalex-snapshot
A Survey of λ Repressor Fragments from Two-State to Downhill Folding
inferred← citeshttps://doi.org/10.1016/j.jsb.2006.11.005openalex-snapshot
Fluctuations of primary ubiquitin folding intermediates in a force clamp
inferred← citeshttps://doi.org/10.1016/j.sbi.2009.12.013openalex-snapshot
Cooperativity and protein folding rates
inferred← citeshttps://doi.org/10.1016/j.sbi.2015.12.001openalex-snapshot
Limited cooperativity in protein folding
inferred← citeshttps://doi.org/10.1021/acs.accounts.0c00322openalex-snapshot
Lessons about Protein Folding and Binding from Archetypal Folds
inferred← citeshttps://doi.org/10.1021/acs.biochem.4c00645openalex-snapshot
Dissecting the Roles of Electrostatic Interactions in Modulating the Folding Stability and Cooperativity of Engrailed Homeodomain
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c05976openalex-snapshot
Slow Folding of a Helical Protein: Large Barriers, Strong Internal Friction, or a Shallow, Bumpy Landscape?
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b09568openalex-snapshot
Bridging Experiments and Native-Centric Simulations of a Downhill Folding Protein
inferred← citeshttps://doi.org/10.1021/acs.jpclett.1c02387openalex-snapshot
Residue-Specific Kinetic Insights into the Transition State in Slow Polypeptide Topological Isomerization by NMR Exchange Spectroscopy
inferred← citeshttps://doi.org/10.1021/acs.jpclett.9b03591openalex-snapshot
Mosaic Cooperativity in Slow Polypeptide Topological Isomerization Revealed by Residue-Specific NMR Thermodynamic Analysis
inferred← citeshttps://doi.org/10.1021/acsomega.5c05567openalex-snapshot
FitFoldData: A Web-Based Toolkit for Circular Dichroism and Differential Scanning Calorimetry Data Analysis of Protein Thermal Denaturation
inferred← citeshttps://doi.org/10.1021/bi060643copenalex-snapshot
Dynamics, Energetics, and Structure in Protein Folding
inferred← citeshttps://doi.org/10.1021/ct300676wopenalex-snapshot
Predictions from an Ising-like Statistical Mechanical Model on the Dynamic and Thermodynamic Effects of Protein Surface Electrostatics
inferred← citeshttps://doi.org/10.1021/ja0689740openalex-snapshot
Protein Folding Kinetics: Barrier Effects in Chemical and Thermal Denaturation Experiments
inferred← citeshttps://doi.org/10.1021/ja100815aopenalex-snapshot
Analyzing Protein Folding Cooperativity by Differential Scanning Calorimetry and NMR Spectroscopy
inferred← citeshttps://doi.org/10.1021/ja103612qopenalex-snapshot
Navigating the Downhill Protein Folding Regime via Structural Homologues
inferred← citeshttps://doi.org/10.1021/ja204053nopenalex-snapshot
The Native Ensemble and Folding of a Protein Molten-Globule: Functional Consequence of Downhill Folding
inferred← citeshttps://doi.org/10.1021/ja4009562openalex-snapshot
Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins
inferred← citeshttps://doi.org/10.1021/ja502705yopenalex-snapshot
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
inferred← citeshttps://doi.org/10.1021/ja801401aopenalex-snapshot
Expanding the Realm of Ultrafast Protein Folding: gpW, a Midsize Natural Single-Domain with α+β Topology that Folds Downhill
inferred← citeshttps://doi.org/10.1021/jp0757715openalex-snapshot
Estimating Free-Energy Barrier Heights for an Ultrafast Folding Protein from Calorimetric and Kinetic Data
inferred← citeshttps://doi.org/10.1021/jp200296vopenalex-snapshot
Denaturation Behaviors of Two-State and Non-Two-State Proteins Examined by an Interruption–Incubation Protocol
inferred← citeshttps://doi.org/10.1021/jp212132vopenalex-snapshot
Configuration-Dependent Diffusion Dynamics of Downhill and Two-State Protein Folding
inferred← citeshttps://doi.org/10.1021/jp400174eopenalex-snapshot
Sub-millisecond Chain Collapse of the Escherichia coli Globin ApoHmpH
inferred← citeshttps://doi.org/10.1021/jp504261gopenalex-snapshot
Thermodynamics of Downhill Folding: Multi-Probe Analysis of PDD, a Protein that Folds Over a Marginal Free Energy Barrier
inferred← citeshttps://doi.org/10.1021/la1012389openalex-snapshot
Secondary Structure Specific Entropy Change of a Partially Unfolded Protein Molecule
inferred← citeshttps://doi.org/10.1038/s41586-018-0820-9openalex-snapshot
Chemical control of structure and guest uptake by a conformationally mobile porous material
inferred← citeshttps://doi.org/10.1038/s42005-022-01125-5openalex-snapshot
Compliant mechanical response of the ultrafast folding protein EnHD under force
inferred← citeshttps://doi.org/10.1039/c1cp20156eopenalex-snapshot
Estimation of protein folding free energy barriers from calorimetric data by multi-model Bayesian analysis
inferred← citeshttps://doi.org/10.1039/c1cp20402eopenalex-snapshot
Integrated prediction of protein folding and unfolding rates from only size and structural class
inferred← citeshttps://doi.org/10.1039/c3sm51439kopenalex-snapshot
Single molecule force spectroscopy reveals the temperature-dependent robustness and malleability of a hyperthermophilic protein
inferred← citeshttps://doi.org/10.1039/c4cp06102kopenalex-snapshot
Imprints of function on the folding landscape: functional role for an intermediate in a conserved eukaryotic binding protein
inferred← citeshttps://doi.org/10.1039/c7cp04380eopenalex-snapshot
Roles of conformational disorder and downhill folding in modulating protein–DNA recognition
inferred← citeshttps://doi.org/10.1039/d0cp01758bopenalex-snapshot
Non-specific DNA-driven quinary interactions promote structural transitions in proteins
inferred← citeshttps://doi.org/10.1039/d0cp06560aopenalex-snapshot
First-passage times in protein folding: exploring the native-like states vs. overcoming the free energy barrier
inferred← citeshttps://doi.org/10.1039/d2sc00345gopenalex-snapshot
Structural and dynamical determinants of a β-sheet-enriched intermediate involved in amyloid fibrillar assembly of human prion protein
inferred← citeshttps://doi.org/10.1042/bcj20160107openalex-snapshot
When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches
inferred← citeshttps://doi.org/10.1063/1.2434966openalex-snapshot
Transition-event durations in one-dimensional activated processes
inferred← citeshttps://doi.org/10.1063/1.2780154openalex-snapshot
Influence of the native topology on the folding barrier for small proteins
inferred← citeshttps://doi.org/10.1063/1.3089708openalex-snapshot
Topology-based potentials and the study of the competition between protein folding and aggregation
inferred← citeshttps://doi.org/10.1063/1.5046692openalex-snapshot
Transition-path properties for folding reactions in the limit of small barriers
inferred← citeshttps://doi.org/10.1073/pnas.0609717104openalex-snapshot
Distinguishing between cooperative and unimodal downhill protein folding
inferred← citeshttps://doi.org/10.1073/pnas.0709881105openalex-snapshot
Large-scale modulation of thermodynamic protein folding barriers linked to electrostatics
inferred← citeshttps://doi.org/10.1073/pnas.1005415107openalex-snapshot
Extremely slow intramolecular diffusion in unfolded protein L
inferred← citeshttps://doi.org/10.1073/pnas.1212842109openalex-snapshot
Topography of funneled landscapes determines the thermodynamics and kinetics of protein folding
inferred← citeshttps://doi.org/10.1073/pnas.1506309112openalex-snapshot
Sequence, structure, and cooperativity in folding of elementary protein structural motifs
inferred← citeshttps://doi.org/10.1074/jbc.m111.304386openalex-snapshot
Ensemble Perspective for Catalytic Promiscuity
inferred← citeshttps://doi.org/10.1074/jbc.m112.445767openalex-snapshot
Enzymatic Detoxication, Conformational Selection, and the Role of Molten Globule Active Sites
inferred← citeshttps://doi.org/10.1080/00268976.2018.1496290openalex-snapshot
The characteristics of molten globule states and folding pathways strongly depend on the sequence of a protein
inferred← citeshttps://doi.org/10.1093/nar/gkae1104openalex-snapshot
Circular oligomeric particles formed by Ros/MucR family members mediate DNA organization in α-proteobacteria
inferred← citeshttps://doi.org/10.1146/annurev-biophys-051309-103835openalex-snapshot
Theoretical Perspectives on Protein Folding
inferred← citeshttps://doi.org/10.1146/annurev-physchem-032210-103504openalex-snapshot
Probing Free-Energy Surfaces with Differential Scanning Calorimetry
inferred← citeshttps://doi.org/10.1146/annurev.biochem.77.060706.093102openalex-snapshot
Single-Molecule Studies of Protein Folding
inferred← citeshttps://doi.org/10.1146/annurev.biophys.36.040306.132608openalex-snapshot
Conformational Dynamics and Ensembles in Protein Folding
inferred← citeshttps://doi.org/10.1360/n972016-00531openalex-snapshot
Recent progress in protein and protein-related systems using DSC techniques
inferred← citeshttps://doi.org/10.1371/journal.pone.0078044openalex-snapshot
Slow Proton Transfer Coupled to Unfolding Explains the Puzzling Results of Single-Molecule Experiments on BBL, a Paradigmatic Downhill Folding Protein
inferred← citeshttps://doi.org/10.1371/journal.pone.0085185openalex-snapshot
A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation
inferred← citeshttps://doi.org/10.2142/biophysico.bppb-v20.0046openalex-snapshot
Residue-based correlation between equilibrium and rate constants is an experimental formulation of the consistency principle for smooth structural changes of proteins
inferred← citeshttps://doi.org/10.2976/1.2988030openalex-snapshot
Exploiting the downhill folding regime via experiment
inferred← citeshttps://doi.org/10.3390/biophysica4020016openalex-snapshot
Differential Scanning Calorimetry of Proteins and the Two-State Model: Comparison of Two Formulas
inferred← citeshttps://doi.org/10.48550/arxiv.1007.3029openalex-snapshot
Theoretical Perspectives on Protein Folding
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.