Research graph
References from Examining Protein Residue-Level Stability Using Theory and Experiment. Local targets link to admitted publications; unresolved targets remain external evidence.
Principles that govern the folding of protein chains
10.1126/science.181.4096.223 · 1973 · External reference
How to Fold Graciously
1969 · External reference
Frustration in Biomolecules
10.1017/s0033583514000092 · 2014 · External reference
Entropic barriers, transition states, funnels, and exponential protein folding kinetics: A simple model
10.1110/ps.9.3.452 · 2000 · External reference
Evidence for the principle of minimal frustration in the evolution of protein folding landscapes
10.1073/pnas.1613892114 · 2017 · External reference
Gradual compaction of the nascent peptide during cotranslational folding on the ribosome
10.7554/elife.60895 · 2020 · External reference
Accurate prediction of protein folding mechanisms by simple structure-based statistical mechanical models
10.1038/s41467-023-41664-1 · 2023 · External reference
Localizing frustration in native proteins and protein assemblies
10.1073/pnas.0709915104 · 2007 · External reference
Protein stability engineering insights revealed by domain-wide comprehensive mutagenesis
10.1073/pnas.1903888116 · 2019 · External reference
Local energetic frustration conservation in protein families and superfamilies
10.1038/s41467-023-43801-2 · 2023 · External reference
SOD1 exhibits allosteric frustration to facilitate metal binding affinity
10.1073/pnas.1216597110 · 2013 · External reference
Local frustration around enzyme active sites
10.1073/pnas.1819859116 · 2019 · External reference
A contact-based analysis of local energetic frustration dynamics identifies key residues enabling RfaH fold-switch
10.1002/pro.5182 · 2024 · External reference
Assessing and enhancing foldability in designed proteins
10.1002/pro.4400 · 2022 · External reference
Evolution of frustrated and stabilising contacts in reconstructed ancient proteins
10.1007/s00249-021-01500-0 · 2021 · External reference
Mega-scale experimental analysis of protein folding stability in biology and design
10.1038/s41586-023-06328-6 · 2023 · External reference
The genetic architecture of protein stability
10.1038/s41586-024-07966-0 · 2024 · External reference
Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding
10.1016/j.cell.2020.08.012 · 2020 · External reference
Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics
10.1126/science.abf8761 · 2021 · External reference
The energetic and allosteric landscape for KRAS inhibition
10.1038/s41586-023-06954-0 · 2024 · External reference
Site-saturation mutagenesis of 500 human protein domains
10.1038/s41586-024-08370-4 · 2025 · External reference
Surveying biomolecular frustration at atomic resolution
10.1038/s41467-020-19560-9 · 2020 · External reference
Identification of the Contact Surface of a Streptococcal Protein G Domain Complexed with a Human Fc Fragment
10.1006/jmbi.1993.1514 · 1993 · External reference
Protein Frustratometer 2: a tool to localize energetic frustration in protein molecules, now with electrostatics
10.1093/nar/gkw304 · 2016 · External reference
DeepDDG: Predicting the Stability Change of Protein Point Mutations Using Neural Networks
10.1021/acs.jcim.8b00697 · 2019 · External reference
PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality
10.1186/1471-2105-12-151 · 2011 · External reference
Structure-based self-supervised learning enables ultrafast protein stability prediction upon mutation
10.1016/j.xinn.2024.100750 · 2025 · External reference
FrustratometeR: an R-package to compute local frustration in protein structures, point mutants and MD simulations
10.1093/bioinformatics/btab176 · 2021 · External reference
Highly accurate protein structure prediction with AlphaFold
10.1038/s41586-021-03819-2 · 2021 · External reference
Localizing Frustration in Proteins Using All-Atom Energy Functions
10.1021/acs.jpcb.9b01545 · 2019 · External reference
Structural Equation Models with Non Normal Variables: Problems and remedies
1995 · External reference
Statistical mechanics of proteins with “evolutionary selected” sequences
10.1103/physreve.50.1303 · 1994 · External reference
Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection
10.1073/pnas.1413575111 · 2014 · External reference
Unresolved reference
1987 · External reference
Insights into protein folding mechanisms from large scale analysis of mutational effects
10.1073/pnas.1000988107 · 2010 · External reference
The past, present and future of de novo protein design
10.1038/s41586-026-10328-7 · 2026 · External reference
ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information1
10.1006/jmbi.2000.4474 · 2001 · External reference
Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
10.1002/(sici)1096-987x(199802)19:3<319::aid-jcc6>3.0.co;2-w · 1998 · External reference
UCSF ChimeraX: Structure visualization for researchers, educators, and developers
10.1002/pro.3943 · 2021 · External reference
Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
10.1002/(sici)1096-987x(199802)19:3<319::aid-jcc6>3.0.co;2-w · ExternalCitation · doi-reference
UCSF ChimeraX: Structure visualization for researchers, educators, and developers
10.1002/pro.3943 · ExternalCitation · doi-reference
Assessing and enhancing foldability in designed proteins
10.1002/pro.4400 · ExternalCitation · doi-reference
A contact-based analysis of local energetic frustration dynamics identifies key residues enabling RfaH fold-switch
10.1002/pro.5182 · ExternalCitation · doi-reference
Identification of the Contact Surface of a Streptococcal Protein G Domain Complexed with a Human Fc Fragment
10.1006/jmbi.1993.1514 · ExternalCitation · doi-reference
ConSurf: an algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information1
10.1006/jmbi.2000.4474 · ExternalCitation · doi-reference
Evolution of frustrated and stabilising contacts in reconstructed ancient proteins
10.1007/s00249-021-01500-0 · ExternalCitation · doi-reference
Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding
10.1016/j.cell.2020.08.012 · ExternalCitation · doi-reference
Structure-based self-supervised learning enables ultrafast protein stability prediction upon mutation
10.1016/j.xinn.2024.100750 · ExternalCitation · doi-reference
Frustration in Biomolecules
10.1017/s0033583514000092 · ExternalCitation · doi-reference
DeepDDG: Predicting the Stability Change of Protein Point Mutations Using Neural Networks
10.1021/acs.jcim.8b00697 · ExternalCitation · doi-reference
Localizing Frustration in Proteins Using All-Atom Energy Functions
10.1021/acs.jpcb.9b01545 · ExternalCitation · doi-reference
Surveying biomolecular frustration at atomic resolution
10.1038/s41467-020-19560-9 · ExternalCitation · doi-reference
Accurate prediction of protein folding mechanisms by simple structure-based statistical mechanical models
10.1038/s41467-023-41664-1 · ExternalCitation · doi-reference
Local energetic frustration conservation in protein families and superfamilies
10.1038/s41467-023-43801-2 · ExternalCitation · doi-reference
Highly accurate protein structure prediction with AlphaFold
10.1038/s41586-021-03819-2 · ExternalCitation · doi-reference
Mega-scale experimental analysis of protein folding stability in biology and design
10.1038/s41586-023-06328-6 · ExternalCitation · doi-reference
The energetic and allosteric landscape for KRAS inhibition
10.1038/s41586-023-06954-0 · ExternalCitation · doi-reference
The genetic architecture of protein stability
10.1038/s41586-024-07966-0 · ExternalCitation · doi-reference
Site-saturation mutagenesis of 500 human protein domains
10.1038/s41586-024-08370-4 · ExternalCitation · doi-reference
The past, present and future of de novo protein design
10.1038/s41586-026-10328-7 · ExternalCitation · doi-reference
Localizing frustration in native proteins and protein assemblies
10.1073/pnas.0709915104 · ExternalCitation · doi-reference
Insights into protein folding mechanisms from large scale analysis of mutational effects
10.1073/pnas.1000988107 · ExternalCitation · doi-reference
SOD1 exhibits allosteric frustration to facilitate metal binding affinity
10.1073/pnas.1216597110 · ExternalCitation · doi-reference
Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection
10.1073/pnas.1413575111 · ExternalCitation · doi-reference
Evidence for the principle of minimal frustration in the evolution of protein folding landscapes
10.1073/pnas.1613892114 · ExternalCitation · doi-reference
Local frustration around enzyme active sites
10.1073/pnas.1819859116 · ExternalCitation · doi-reference
Protein stability engineering insights revealed by domain-wide comprehensive mutagenesis
10.1073/pnas.1903888116 · ExternalCitation · doi-reference
FrustratometeR: an R-package to compute local frustration in protein structures, point mutants and MD simulations
10.1093/bioinformatics/btab176 · ExternalCitation · doi-reference
Protein Frustratometer 2: a tool to localize energetic frustration in protein molecules, now with electrostatics
10.1093/nar/gkw304 · ExternalCitation · doi-reference
Statistical mechanics of proteins with “evolutionary selected” sequences
10.1103/physreve.50.1303 · ExternalCitation · doi-reference
Entropic barriers, transition states, funnels, and exponential protein folding kinetics: A simple model
10.1110/ps.9.3.452 · ExternalCitation · doi-reference
Principles that govern the folding of protein chains
10.1126/science.181.4096.223 · ExternalCitation · doi-reference
Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics
10.1126/science.abf8761 · ExternalCitation · doi-reference
PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality
10.1186/1471-2105-12-151 · ExternalCitation · doi-reference
Gradual compaction of the nascent peptide during cotranslational folding on the ribosome
10.7554/elife.60895 · ExternalCitation · doi-reference
