Research graph
References from Unraveling protein folding and structural dynamics. Local targets link to admitted publications; unresolved targets remain external evidence.
Unresolved reference
2015 · External reference
Biophysical insights into pH-induced structural dynamics of recombinant interferon β-1b: aggregation under acidic conditions
2025 · External reference
Unveiling invisible protein states with NMR spectroscopy
10.1016/j.sbi.2019.10.008 · 2020 · External reference
Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins
10.1007/s12551-017-0346-7 · 2018 · External reference
How does protein folding get started?
10.1016/0968-0004(89)90067-4 · 1989 · External reference
Amyloid-induced neurodegeneration: a comprehensive review through aggregomics perception of proteins in health and pathology
10.1016/j.arr.2024.102276 · 2024 · External reference
Monitoring protein aggregation during thermal unfolding in circular dichroism experiments
10.1110/ps.051917406 · 2006 · External reference
Protein data bank (PDB): fifty-three years young and having a transformative impact on science and society
10.1017/s0033583525000034 · 2025 · External reference
Heterogeneity in protein folding and unfolding reactions
10.1021/acs.chemrev.1c00704 · 2022 · External reference
The role of dynamic conformational ensembles in biomolecular recognition
10.1038/nchembio.232 · 2009 · External reference
Transient misfolding dominates multidomain protein folding
10.1038/ncomms9861 · 2015 · External reference
Markov state models with weighted ensemble simulation: how to eliminate the trajectory merging bias
10.1021/acs.jctc.4c01141 · 2025 · External reference
Proteins that switch folds
10.1016/j.sbi.2010.06.002 · 2010 · External reference
Funnels, pathways, and the energy landscape of protein folding: a synthesis
10.1002/prot.340210302 · 1995 · External reference
The dynamical nature of enzymatic catalysis
10.1021/ar5002928 · 2015 · External reference
Dynamic allostery: evolution’s double-edged sword in protein function and disease
10.1016/j.jmb.2025.169175 · 2025 · External reference
Direct observation of the three-state folding of a single protein molecule
10.1126/science.1116702 · 2005 · External reference
Submillisecond protein folding kinetics studied by ultrarapid mixing
10.1073/pnas.94.5.1779 · 1997 · External reference
Peptide self-assembly: from ordered to disordered
10.1021/acs.accounts.3c00592 · 2024 · External reference
Cryo-EM analyses permit visualization of structural polymorphism of biological macromolecules
10.3389/fbinf.2021.788308 · 2021 · External reference
Broadband multidimensional spectroscopy identifies the amide II vibrations in silkworm films
10.3390/molecules27196275 · 2022 · External reference
Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) study on the structure of sodium caseinate in dispersions and at the oil-water interface: effect of calcium ions
10.1016/j.foostr.2022.100276 · 2022 · External reference
Single-particle cryo-EM at crystallographic resolution
10.1016/j.cell.2015.03.049 · 2015 · External reference
Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse
10.1073/pnas.022387699 · 2002 · External reference
Validating molecular dynamics simulations against experimental observables in light of underlying conformational ensembles
10.1021/acs.jpcb.8b02144 · 2018 · External reference
Insights from molecular dynamics simulations for computational protein design
10.1039/c6me00083e · 2017 · External reference
Protein misfolding, functional amyloid, and human disease
10.1146/annurev.biochem.75.101304.123901 · 2006 · External reference
Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade
10.1146/annurev-biochem-061516-045115 · 2017 · External reference
Coarse-grained models of protein folding: toy models or predictive tools?
10.1016/j.sbi.2007.10.005 · 2008 · External reference
Quinary interactions with an unfolded state ensemble
10.1002/pro.3206 · 2017 · External reference
Metalloprotein active site structure determination: synergy between X-ray absorption spectroscopy and X-ray crystallography
10.1016/j.jinorgbio.2012.06.019 · 2012 · External reference
Ensemble versus single-molecule protein unfolding
10.1073/pnas.0501773102 · 2005 · External reference
Molecular dynamics simulations of voltage-gated cation channels: insights on voltage-sensor domain function and modulation
10.3389/fphar.2012.00097 · 2012 · External reference
Unresolved reference
2019 · External reference
Temperature-resolved crystallography reveals rigid-body dominance over local flexibility in B-factors
10.1021/acsomega.5c04454 · 2025 · External reference
The protein folding problem: when will it be solved?
10.1016/j.sbi.2007.06.001 · 2007 · External reference
Direct molecular dynamics observation of protein folding transition state ensemble
10.1016/s0006-3495(02)75352-6 · 2002 · External reference
Understanding protein folding via free-energy surfaces from theory and experiment
10.1016/s0968-0004(00)01610-8 · 2000 · External reference
Protein misfolding, evolution and disease
10.1016/s0968-0004(99)01445-0 · 1999 · External reference
Structural dynamics of glutamate signaling systems by smFRET
10.1016/j.bpj.2020.10.009 · 2020 · External reference
Effects of external perturbations on protein systems: a microscopic view
10.1021/acsomega.2c06199 · 2022 · External reference
The nature of protein folding pathways
10.1073/pnas.1411798111 · 2014 · External reference
Visualizing protein folding and unfolding
10.1016/j.jmb.2019.02.026 · 2019 · External reference
Φ-Value analysis and the nature of protein-folding transition states
10.1073/pnas.0402684101 · 2004 · External reference
Insights into the mechanism of tryptophan fluorescence quenching due to synthetic crowding agents: a combined experimental and computational study
10.1021/acsomega.3c06006 · 2023 · External reference
Fuzziness and frustration in the energy landscape of protein folding, function, and assembly
10.1021/acs.accounts.0c00813 · 2021 · External reference
Circular dichroism and its empirical application to biopolymers
2006 · External reference
Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
10.1038/nprot.2006.204 · 2006 · External reference
Adaptability of protein structures to enable functional interactions and evolutionary implications
10.1016/j.sbi.2015.07.007 · 2015 · External reference
Characterizing metal-binding sites in proteins with X-ray crystallography
10.1038/nprot.2018.018 · 2018 · External reference
Extrinsic fluorescent dyes as tools for protein characterization
10.1007/s11095-007-9516-9 · 2008 · External reference
Bridging protein structure, dynamics, and function using hydrogen/deuterium-exchange mass spectrometry
10.1002/pro.3790 · 2020 · External reference
Measuring the average shape of transition paths during the folding of a single biological molecule
10.1016/j.bpj.2018.11.1766 · 2019 · External reference
Molecular dynamics simulation for All
10.1016/j.neuron.2018.08.011 · 2018 · External reference
NMR-based methods for protein analysis
10.1021/acs.analchem.0c03830 · 2021 · External reference
Unresolved reference
2024 · External reference
Hydrophobicity of proteins and interfaces: insights from density fluctuations
10.1146/annurev-chembioeng-061010-114156 · 2011 · External reference
High-resolution protein modeling through Cryo-EM and AI: current trends and future perspectives – a review
10.3389/fmolb.2025.1688455 · 2025 · External reference
Molecular dynamics simulations of biomolecules
10.1038/nsb0902-646 · 2002 · External reference
The time revolution in macromolecular crystallography
10.1063/4.0000247 · 2024 · External reference
Protein flexibility and enzymatic catalysis
10.1016/b978-0-12-398312-1.00007-x · 2012 · External reference
Nuclear magnetic resonance studies of proteins
10.1016/s0021-9258(19)73941-6 · 1962 · External reference
Ligand binding introduces significant allosteric shifts in the locations of protein fluctuations
10.3389/fmolb.2021.733148 · 2021 · External reference
Unresolved reference
2023 · External reference
Single-molecule Förster resonance energy transfer study of protein dynamics under denaturing conditions
10.1073/pnas.0507728102 · 2005 · External reference
Are there pathways for protein folding?
10.1051/jcp/1968650044 · 1968 · External reference
Unlocking insights into folding, structure, and function of proteins through circular dichroism spectroscopy—a short review
10.3390/applbiosci2040040 · 2023 · External reference
Unresolved reference
2012 · External reference
Protein dynamics: dancing on an ever-changing free energy stage
10.1016/j.coph.2010.09.015 · 2010 · External reference
The folding and misfolding mechanisms of multidomain proteins
10.1016/j.medidd.2022.100126 · 2022 · External reference
Protein stability: computation, sequence statistics, and new experimental methods
10.1016/j.sbi.2015.09.002 · 2015 · External reference
How cooperative are protein folding and unfolding transitions?
10.1002/pro.3015 · 2016 · External reference
Energy landscape in protein folding and unfolding
10.1073/pnas.1524864113 · 2016 · External reference
Mixed mechanism of conformational selection and induced fit as a molecular recognition process in the calreticulin family of proteins
10.1371/journal.pcbi.1010661 · 2022 · External reference
Visualizing protein breathing motions associated with aromatic ring flipping
10.1038/s41586-022-04417-6 · 2022 · External reference
Introducing the levinthal’s protein folding paradox and its solution
10.1021/ed300302h · 2014 · External reference
Substantial increase of protein stability by multiple disulphide bonds
10.1038/342291a0 · 1989 · External reference
Protein X-ray crystallography and drug discovery
10.3390/molecules25051030 · 2020 · External reference
Comparing proteins by their internal dynamics: exploring structure–function relationships beyond static structural alignments
10.1016/j.plrev.2012.10.009 · 2013 · External reference
Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories
10.1038/s41467-017-01996-1 · 2017 · External reference
Uncovering protein function: from classification to complexes
10.1042/ebc20200108 · 2022 · External reference
Atomic force microscopy-based force spectroscopy and multiparametric imaging of biomolecular and cellular systems
10.1021/acs.chemrev.0c00617 · 2021 · External reference
Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy
10.1038/nmeth.1218 · 2008 · External reference
Measuring the local velocity along transition paths during the folding of single biological molecules
10.1103/physrevlett.121.018102 · 2018 · External reference
How general is the nucleation-condensation mechanism?
10.1002/prot.22099 · 2008 · External reference
Dynamic connection between enzymatic catalysis and collective protein motions
10.1021/acs.biochem.1c00221 · 2021 · External reference
Theory of protein folding: the energy landscape perspective
10.1146/annurev.physchem.48.1.545 · 1997 · External reference
Circular dichroism spectroscopy in protein engineering and pharmaceutical development: applications in structural characterization and quality assessment
10.1016/j.pep.2025.106826 · 2026 · External reference
Protein ionizable groups: pK values and their contribution to protein stability and solubility
10.1074/jbc.r800080200 · 2009 · External reference
Forces stabilizing proteins
10.1016/j.febslet.2014.05.006 · 2014 · External reference
Molecular recognition in chemical and biological systems
10.1002/anie.201408487 · 2015 · External reference
Single-molecule force spectroscopy of protein folding
10.1016/j.jmb.2021.167207 · 2021 · External reference
Backbone-Backbone H-bonds make context-dependent contributions to protein folding kinetics and thermodynamics: lessons from amide-to-ester mutations
10.1016/s0065-3233(05)72002-7 · 2005 · External reference
10.1038/s41592-019-0506-8
10.1038/s41592-019-0506-8 · 2019 · External reference
Stability and folding studies of the N-domain of troponin C. Evidence for the formation of an intermediate
10.1016/j.abb.2004.05.002 · 2004 · External reference
Unresolved reference
2024 · External reference
Mapping protein dynamics by X-ray diffraction
10.1016/0079-6107(85)90002-1 · 1985 · External reference
A backbone-based theory of protein folding
10.1073/pnas.0606843103 · 2006 · External reference
Van der Waals interactions involving proteins
10.1016/s0006-3495(96)79641-8 · 1996 · External reference
Integrative computational approaches for the discovery of triazole-based urease inhibitors: a machine learning, virtual screening, and meta-dynamics framework
10.3390/ijms262311576 · 2025 · External reference
How fast is protein hydrophobic collapse?
10.1073/pnas.2033863100 · 2003 · External reference
Single-molecule fluorescence resonance energy transfer in molecular biology
10.1039/c6nr06794h · 2016 · External reference
Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically disordered proteins
10.1146/annurev-biophys-062215-010915 · 2016 · External reference
Protein dynamics and enzymatic catalysis
10.1021/acs.jpcb.3c00477 · 2023 · External reference
Hybrid methods for combined experimental and computational determination of protein structure
10.1063/5.0026025 · 2020 · External reference
Why do proteins fold into unique 3D structures? And other questions
10.1134/s1990793123030259 · 2023 · External reference
Nonnative contact effects in protein folding
10.1039/c8cp07524g · 2019 · External reference
Atomic-level characterization of the structural dynamics of proteins
10.1126/science.1187409 · 2010 · External reference
A glimpse of structural biology through X-ray crystallography
10.1016/j.cell.2014.10.051 · 2014 · External reference
Exploring functional groups and molecular structures: a comprehensive analysis using FTIR spectroscopy
2024 · External reference
UV-visible spectroscopy: a review on its pharmaceutical and bio-allied sciences applications
10.2174/0115734129300562240408042614 · 2024 · External reference
Unresolved reference
2025 · External reference
Is protein folding a thermodynamically unfavorable, active, energy-dependent process?
10.3390/ijms23010521 · 2022 · External reference
FTIR investigation of the secondary structure of type I collagen: new insight into the amide III band
10.1016/j.saa.2019.118006 · 2020 · External reference
Dynamic light scattering: a practical guide and applications in biomedical sciences
10.1007/s12551-016-0218-6 · 2016 · External reference
The complex folding network of single calmodulin molecules
10.1126/science.1207598 · 2011 · External reference
The path to solving the protein folding problem
10.2144/btn-2023-0031 · 2023 · External reference
Modern technologies of solution nuclear magnetic resonance spectroscopy for three-dimensional structure determination of proteins open avenues for life scientists
10.1016/j.csbj.2017.04.001 · 2017 · External reference
Protein folding mechanism revealed by single-molecule force spectroscopy experiments
10.52601/bpr.2021.210024 · 2021 · External reference
Conformational heterogeneity and probability distributions from single-particle cryo-electron microscopy
10.1016/j.sbi.2023.102626 · 2023 · External reference
Protein stability, flexibility and function
10.1016/j.bbapap.2010.11.005 · 2011 · External reference
Dynamic structural science: recent developments in time-resolved spectroscopy and X-ray crystallography
10.1042/bst20130125 · 2013 · External reference
Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions
10.2174/9781608054640113060014 · 2012 · External reference
The hydrophobic temperature dependence of amino acids directly calculated from protein structures
10.1371/journal.pcbi.1004277 · 2015 · External reference
Exploring cryo-electron microscopy with molecular dynamics
10.1042/bst20210485 · 2022 · External reference
Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties
10.1016/s1359-0278(97)00002-3 · 1997 · External reference
Measuring multisubunit mechanics of geometrically programmed colloidal assemblies via cryo-EM multi-body refinement
10.1073/pnas.2500716122 · 2025 · External reference
Topography of funneled landscapes determines the thermodynamics and kinetics of protein folding
10.1073/pnas.1212842109 · 2012 · External reference
Protein ensembles: how does nature harness thermodynamic fluctuations for life? The diverse functional roles of conformational ensembles in the cell
10.1021/acs.chemrev.5b00562 · 2016 · External reference
Unresolved reference
2016 · External reference
Identification of protein interactions involved in cellular signaling
10.1074/mcp.r113.027771 · 2013 · External reference
Recent developments in the electronic spectroscopy of amides and α-helical polypeptides
10.1016/s0301-4622(02)00187-4 · 2002 · External reference
Förster resonance energy transfer (FRET)-based small-molecule sensors and imaging agents
10.1039/c9cs00318e · 2020 · External reference
The free energy landscape of protein folding and dynamics: a global view
10.1080/07391102.2012.748536 · 2013 · External reference
Protein dynamics and motions in relation to their functions: several case studies and the underlying mechanisms
10.1080/07391102.2013.770372 · 2014 · External reference
Estimation of peptide helicity from circular dichroism using the ensemble model
10.1021/acs.jpcb.3c07511 · 2024 · External reference
Unresolved reference
External reference
Progressive assembly of multi-domain protein structures from cryo-EM density maps
10.1038/s43588-022-00232-1 · 2022 · External reference
Protein functional landscapes, dynamics, allostery: a tortuous path towards a universal theoretical framework
10.1017/s0033583510000119 · 2010 · External reference
Molecular recognition in chemical and biological systems
10.1002/anie.201408487 · ExternalCitation · doi-reference
How cooperative are protein folding and unfolding transitions?
10.1002/pro.3015 · ExternalCitation · doi-reference
Quinary interactions with an unfolded state ensemble
10.1002/pro.3206 · ExternalCitation · doi-reference
Bridging protein structure, dynamics, and function using hydrogen/deuterium-exchange mass spectrometry
10.1002/pro.3790 · ExternalCitation · doi-reference
How general is the nucleation-condensation mechanism?
10.1002/prot.22099 · ExternalCitation · doi-reference
Funnels, pathways, and the energy landscape of protein folding: a synthesis
10.1002/prot.340210302 · ExternalCitation · doi-reference
Extrinsic fluorescent dyes as tools for protein characterization
10.1007/s11095-007-9516-9 · ExternalCitation · doi-reference
Dynamic light scattering: a practical guide and applications in biomedical sciences
10.1007/s12551-016-0218-6 · ExternalCitation · doi-reference
Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins
10.1007/s12551-017-0346-7 · ExternalCitation · doi-reference
Mapping protein dynamics by X-ray diffraction
10.1016/0079-6107(85)90002-1 · ExternalCitation · doi-reference
How does protein folding get started?
10.1016/0968-0004(89)90067-4 · ExternalCitation · doi-reference
Protein flexibility and enzymatic catalysis
10.1016/b978-0-12-398312-1.00007-x · ExternalCitation · doi-reference
Stability and folding studies of the N-domain of troponin C. Evidence for the formation of an intermediate
10.1016/j.abb.2004.05.002 · ExternalCitation · doi-reference
Amyloid-induced neurodegeneration: a comprehensive review through aggregomics perception of proteins in health and pathology
10.1016/j.arr.2024.102276 · ExternalCitation · doi-reference
Protein stability, flexibility and function
10.1016/j.bbapap.2010.11.005 · ExternalCitation · doi-reference
Measuring the average shape of transition paths during the folding of a single biological molecule
10.1016/j.bpj.2018.11.1766 · ExternalCitation · doi-reference
Structural dynamics of glutamate signaling systems by smFRET
10.1016/j.bpj.2020.10.009 · ExternalCitation · doi-reference
A glimpse of structural biology through X-ray crystallography
10.1016/j.cell.2014.10.051 · ExternalCitation · doi-reference
Single-particle cryo-EM at crystallographic resolution
10.1016/j.cell.2015.03.049 · ExternalCitation · doi-reference
Protein dynamics: dancing on an ever-changing free energy stage
10.1016/j.coph.2010.09.015 · ExternalCitation · doi-reference
Modern technologies of solution nuclear magnetic resonance spectroscopy for three-dimensional structure determination of proteins open avenues for life scientists
10.1016/j.csbj.2017.04.001 · ExternalCitation · doi-reference
Forces stabilizing proteins
10.1016/j.febslet.2014.05.006 · ExternalCitation · doi-reference
Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) study on the structure of sodium caseinate in dispersions and at the oil-water interface: effect of calcium ions
10.1016/j.foostr.2022.100276 · ExternalCitation · doi-reference
Metalloprotein active site structure determination: synergy between X-ray absorption spectroscopy and X-ray crystallography
10.1016/j.jinorgbio.2012.06.019 · ExternalCitation · doi-reference
Visualizing protein folding and unfolding
10.1016/j.jmb.2019.02.026 · ExternalCitation · doi-reference
Single-molecule force spectroscopy of protein folding
10.1016/j.jmb.2021.167207 · ExternalCitation · doi-reference
Dynamic allostery: evolution’s double-edged sword in protein function and disease
10.1016/j.jmb.2025.169175 · ExternalCitation · doi-reference
The folding and misfolding mechanisms of multidomain proteins
10.1016/j.medidd.2022.100126 · ExternalCitation · doi-reference
Molecular dynamics simulation for All
10.1016/j.neuron.2018.08.011 · ExternalCitation · doi-reference
Circular dichroism spectroscopy in protein engineering and pharmaceutical development: applications in structural characterization and quality assessment
10.1016/j.pep.2025.106826 · ExternalCitation · doi-reference
Comparing proteins by their internal dynamics: exploring structure–function relationships beyond static structural alignments
10.1016/j.plrev.2012.10.009 · ExternalCitation · doi-reference
FTIR investigation of the secondary structure of type I collagen: new insight into the amide III band
10.1016/j.saa.2019.118006 · ExternalCitation · doi-reference
The protein folding problem: when will it be solved?
10.1016/j.sbi.2007.06.001 · ExternalCitation · doi-reference
Coarse-grained models of protein folding: toy models or predictive tools?
10.1016/j.sbi.2007.10.005 · ExternalCitation · doi-reference
Proteins that switch folds
10.1016/j.sbi.2010.06.002 · ExternalCitation · doi-reference
Adaptability of protein structures to enable functional interactions and evolutionary implications
10.1016/j.sbi.2015.07.007 · ExternalCitation · doi-reference
Protein stability: computation, sequence statistics, and new experimental methods
10.1016/j.sbi.2015.09.002 · ExternalCitation · doi-reference
Unveiling invisible protein states with NMR spectroscopy
10.1016/j.sbi.2019.10.008 · ExternalCitation · doi-reference
Conformational heterogeneity and probability distributions from single-particle cryo-electron microscopy
10.1016/j.sbi.2023.102626 · ExternalCitation · doi-reference
Direct molecular dynamics observation of protein folding transition state ensemble
10.1016/s0006-3495(02)75352-6 · ExternalCitation · doi-reference
Van der Waals interactions involving proteins
10.1016/s0006-3495(96)79641-8 · ExternalCitation · doi-reference
Nuclear magnetic resonance studies of proteins
10.1016/s0021-9258(19)73941-6 · ExternalCitation · doi-reference
Backbone-Backbone H-bonds make context-dependent contributions to protein folding kinetics and thermodynamics: lessons from amide-to-ester mutations
10.1016/s0065-3233(05)72002-7 · ExternalCitation · doi-reference
Recent developments in the electronic spectroscopy of amides and α-helical polypeptides
10.1016/s0301-4622(02)00187-4 · ExternalCitation · doi-reference
Understanding protein folding via free-energy surfaces from theory and experiment
10.1016/s0968-0004(00)01610-8 · ExternalCitation · doi-reference
Protein misfolding, evolution and disease
10.1016/s0968-0004(99)01445-0 · ExternalCitation · doi-reference
Protein folding kinetics: timescales, pathways and energy landscapes in terms of sequence-dependent properties
10.1016/s1359-0278(97)00002-3 · ExternalCitation · doi-reference
Protein functional landscapes, dynamics, allostery: a tortuous path towards a universal theoretical framework
10.1017/s0033583510000119 · ExternalCitation · doi-reference
Protein data bank (PDB): fifty-three years young and having a transformative impact on science and society
10.1017/s0033583525000034 · ExternalCitation · doi-reference
Fuzziness and frustration in the energy landscape of protein folding, function, and assembly
10.1021/acs.accounts.0c00813 · ExternalCitation · doi-reference
Peptide self-assembly: from ordered to disordered
10.1021/acs.accounts.3c00592 · ExternalCitation · doi-reference
NMR-based methods for protein analysis
10.1021/acs.analchem.0c03830 · ExternalCitation · doi-reference
Dynamic connection between enzymatic catalysis and collective protein motions
10.1021/acs.biochem.1c00221 · ExternalCitation · doi-reference
Atomic force microscopy-based force spectroscopy and multiparametric imaging of biomolecular and cellular systems
10.1021/acs.chemrev.0c00617 · ExternalCitation · doi-reference
Heterogeneity in protein folding and unfolding reactions
10.1021/acs.chemrev.1c00704 · ExternalCitation · doi-reference
Protein ensembles: how does nature harness thermodynamic fluctuations for life? The diverse functional roles of conformational ensembles in the cell
10.1021/acs.chemrev.5b00562 · ExternalCitation · doi-reference
Markov state models with weighted ensemble simulation: how to eliminate the trajectory merging bias
10.1021/acs.jctc.4c01141 · ExternalCitation · doi-reference
Protein dynamics and enzymatic catalysis
10.1021/acs.jpcb.3c00477 · ExternalCitation · doi-reference
Estimation of peptide helicity from circular dichroism using the ensemble model
10.1021/acs.jpcb.3c07511 · ExternalCitation · doi-reference
Validating molecular dynamics simulations against experimental observables in light of underlying conformational ensembles
10.1021/acs.jpcb.8b02144 · ExternalCitation · doi-reference
Effects of external perturbations on protein systems: a microscopic view
10.1021/acsomega.2c06199 · ExternalCitation · doi-reference
Insights into the mechanism of tryptophan fluorescence quenching due to synthetic crowding agents: a combined experimental and computational study
10.1021/acsomega.3c06006 · ExternalCitation · doi-reference
Temperature-resolved crystallography reveals rigid-body dominance over local flexibility in B-factors
10.1021/acsomega.5c04454 · ExternalCitation · doi-reference
The dynamical nature of enzymatic catalysis
10.1021/ar5002928 · ExternalCitation · doi-reference
Introducing the levinthal’s protein folding paradox and its solution
10.1021/ed300302h · ExternalCitation · doi-reference
Substantial increase of protein stability by multiple disulphide bonds
10.1038/342291a0 · ExternalCitation · doi-reference
The role of dynamic conformational ensembles in biomolecular recognition
10.1038/nchembio.232 · ExternalCitation · doi-reference
Transient misfolding dominates multidomain protein folding
10.1038/ncomms9861 · ExternalCitation · doi-reference
Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy
10.1038/nmeth.1218 · ExternalCitation · doi-reference
Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
10.1038/nprot.2006.204 · ExternalCitation · doi-reference
Characterizing metal-binding sites in proteins with X-ray crystallography
10.1038/nprot.2018.018 · ExternalCitation · doi-reference
Molecular dynamics simulations of biomolecules
10.1038/nsb0902-646 · ExternalCitation · doi-reference
Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories
10.1038/s41467-017-01996-1 · ExternalCitation · doi-reference
Visualizing protein breathing motions associated with aromatic ring flipping
10.1038/s41586-022-04417-6 · ExternalCitation · doi-reference
10.1038/s41592-019-0506-8
10.1038/s41592-019-0506-8 · ExternalCitation · doi-reference
Progressive assembly of multi-domain protein structures from cryo-EM density maps
10.1038/s43588-022-00232-1 · ExternalCitation · doi-reference
Insights from molecular dynamics simulations for computational protein design
10.1039/c6me00083e · ExternalCitation · doi-reference
Single-molecule fluorescence resonance energy transfer in molecular biology
10.1039/c6nr06794h · ExternalCitation · doi-reference
Nonnative contact effects in protein folding
10.1039/c8cp07524g · ExternalCitation · doi-reference
Förster resonance energy transfer (FRET)-based small-molecule sensors and imaging agents
10.1039/c9cs00318e · ExternalCitation · doi-reference
Dynamic structural science: recent developments in time-resolved spectroscopy and X-ray crystallography
10.1042/bst20130125 · ExternalCitation · doi-reference
Exploring cryo-electron microscopy with molecular dynamics
10.1042/bst20210485 · ExternalCitation · doi-reference
Uncovering protein function: from classification to complexes
10.1042/ebc20200108 · ExternalCitation · doi-reference
Are there pathways for protein folding?
10.1051/jcp/1968650044 · ExternalCitation · doi-reference
The time revolution in macromolecular crystallography
10.1063/4.0000247 · ExternalCitation · doi-reference
Hybrid methods for combined experimental and computational determination of protein structure
10.1063/5.0026025 · ExternalCitation · doi-reference
Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse
10.1073/pnas.022387699 · ExternalCitation · doi-reference
Φ-Value analysis and the nature of protein-folding transition states
10.1073/pnas.0402684101 · ExternalCitation · doi-reference
Ensemble versus single-molecule protein unfolding
10.1073/pnas.0501773102 · ExternalCitation · doi-reference
Single-molecule Förster resonance energy transfer study of protein dynamics under denaturing conditions
10.1073/pnas.0507728102 · ExternalCitation · doi-reference
A backbone-based theory of protein folding
10.1073/pnas.0606843103 · ExternalCitation · doi-reference
Topography of funneled landscapes determines the thermodynamics and kinetics of protein folding
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