ArticleJournal of molecular biology2006
Elucidating quantitative stability/flexibility relationships within thioredoxin and its fragments using a distance constraint model.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Protein Function Analysis through Machine Learning.Biomolecules · 2022Review
- Novel Ricin Subunit Antigens With Enhanced Capacity to Elicit Toxin-Neutralizing Antibody Responses in Mice.Journal of pharmaceutical sciences · 2016Article
- Rigidity Emerges during Antibody Evolution in Three Distinct Antibody Systems: Evidence from QSFR Analysis of Fab Fragments.PLoS computational biology · 2015Article
- Thermodynamic stability and flexibility characteristics of antibody fragment complexes.Protein and peptide letters · 2014Article
- Redistribution of flexibility in stabilizing antibody fragment mutants follows Le Châtelier's principle.PloS one · 2014Article
- A case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Variations within class-A β-lactamase physiochemical properties reflect evolutionary and environmental patterns, but not antibiotic specificity.PLoS computational biology · 2013Article
- Ensemble properties of network rigidity reveal allosteric mechanisms.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.PLoS computational biology · 2012Article
- Article
- Characterizing protein motions from structure.Journal of molecular graphics & modelling · 2011Article
- Nonadditivity in the alpha-helix to coil transition.Biopolymers · 2011Article
- Nonadditivity in conformational entropy upon molecular rigidification reveals a universal mechanism affecting folding cooperativity.Biophysical journal · 2011Article
- Ensemble-based methods for describing protein dynamics.Current opinion in pharmacology · 2010Review
- Predicting the melting point of human C-type lysozyme mutants.Current protein & peptide science · 2010Article
- Allosteric response is both conserved and variable across three CheY orthologs.Biophysical journal · 2010Article
- A signal processing method to explore similarity in protein flexibility.Advances in bioinformatics · 2010Article
- Helix/coil nucleation: a local response to global demands.Biophysical journal · 2009Article
- Unifying mechanical and thermodynamic descriptions across the thioredoxin protein family.Proteins · 2009Article
- Conformational Entropy of an Ideal Cross-Linking Polymer Chain.Entropy (Basel, Switzerland) · 2008Article
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Authors and funding
4 authors.
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Abstract
Numerous quantitative stability/flexibility relationships, within Escherichia coli thioredoxin (Trx) and its fragments are determined using a minimal distance constraint model (DCM). A one-dimensional free energy landscape as a function of global flexibility reveals Trx to fold in a low-barrier two-state process, with a voluminous transition state. Near the folding transition temperature, the native free energy basin is markedly skewed to allow partial unfolded forms. Under native conditions the skewed shape is lost, and the protein forms a compact structure with some flexibility. Predictions on ten Trx fragments are generally consistent with experimental observations that they are disordered, and that complementary fragments reconstitute. A hierarchical unfolding pathway is uncovered using an exhaustive computational procedure of breaking interfacial cross-linking hydrogen bonds that span over a series of fragment dissociations. The unfolding pathway leads to a stable core structure (residues 22-90), predicted to act as a kinetic trap. Direct connection between degree of rigidity within molecular structure and non-additivity of free energy is demonstrated using a thermodynamic cycle involving fragments and their hierarchical unfolding pathway. Additionally, the model provides insight about molecular cooperativity within Trx in its native state, and about intermediate states populating the folding/unfolding pathways. Native state cooperativity correlation plots highlight several flexibly correlated regions, giving insight into the catalytic mechanism that facilitates access to the active site disulfide bond. Residual native cooperativity correlations are present in the core substructure, suggesting that Trx can function when it is partly unfolded. This natively disordered kinetic trap, interpreted as a molten globule, has a wide temperature range of metastability, and it is identified as the "slow intermediate state" observed in kinetic experiments. These computational results are found to be in overall agreement with a large array of experimental data.
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