Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations.

Journal of molecular biology - 5 Jul 2002

Guerois Raphael, Nielsen Jens Erik, Serrano Luis

Abstract excerpt

We have developed a computer algorithm, FOLDEF (for FOLD-X energy function), to provide a fast and quantitative estimation of the importance of the interactions contributing to the stability of proteins and protein complexes. The predictive power of FOLDEF was tested on a very large set of point mutants (1088 mutants) spanning most of the structural environments found in proteins. FOLDEF uses a full atomic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Databases as Topic
Share to Hydrogen Bonding
Share to Models, Statistical

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Software

Share to Thermodynamics

Source

Identifiers

PMID: 12079393
DOI: 10.1016/S0022-2836(02)00442-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations.PMID 12079393Read ↗

ProAffiMuSeq: sequence-based method to predict the binding free energy change of protein-protein complexes upon mutation using functional classification.Semantic proximity Read ↗

Predicting the stability of mutant proteins by computational approaches: an overview.Semantic proximity Read ↗

Towards sequence-based prediction of mutation-induced stability changes in unseen non-homologous proteins.Semantic proximity Read ↗

Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details.Semantic proximity Read ↗

Correspondence between functional scores from deep mutational scans and predicted effects on protein stability.Semantic proximity Read ↗

Folding RaCe: a robust method for predicting changes in protein folding rates upon point mutations.Semantic proximity Read ↗

FireProt: web server for automated design of thermostable proteins.Semantic proximity Read ↗

Correspondence between functional scores from deep mutational scans and predicted effects on protein stabilitySemantic proximity Read ↗

Computational approaches for predicting mutant protein stability.Semantic proximity Read ↗

Predicting changes in protein thermostability brought about by single- or multi-site mutations.Semantic proximity Read ↗

The FoldX web server: an online force field.Semantic proximity Read ↗

Four-body scoring function for mutagenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.