ArticleProtein science : a publication of the Protein Society2009
Sequence determinants of thermodynamic stability in a WW domain--an all-beta-sheet protein.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- Structural and energetic analysis of stabilizing indel mutations.bioRxiv : the preprint server for biology · 2024Article
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- The WW domain of IQGAP1 binds directly to the p110α catalytic subunit of PI 3-kinase.The Biochemical journal · 2023Article
- An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnChembiochem : a European journal of chemical biology · 2023Article
- Late-Stage Functionalisation of Peptides on the Solid Phase by an Iodination-Substitution Approach.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Identification of novel functional mini-receptors by combinatorial screening of split-WW domains.Chemical science · 2022Article
- The CSY-protecting group in the microwave-assisted synthesis of aggregation-prone peptides.RSC chemical biology · 2022Article
- PEGylation Increases the Strength of a Nearby NH-π Hydrogen Bond in the WW Domain.Biochemistry · 2021Article
- Funneled energy landscape unifies principles of protein binding and evolution.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational landscape of substituted prolines.Biophysical reviews · 2020Review
- Activity and Affinity of Pin1 Variants.Molecules (Basel, Switzerland) · 2019Review
- Post-Translational Backbone Engineering through Selenomethionine-Mediated Incorporation of Freidinger Lactams.Angewandte Chemie (International ed. in English) · 2018Article
- Polyethylene Glycol Based Changes to β-Sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location.Bioconjugate chemistry · 2017Article
- How Many Protein Sequences Fold to a Given Structure? A Coevolutionary Analysis.Biophysical journal · 2017Article
- Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.Accounts of chemical research · 2017Article
- Global analysis of protein folding using massively parallel design, synthesis, and testing.Science (New York, N.Y.) · 2017Article
- The WW domain of the scaffolding protein IQGAP1 is neither necessary nor sufficient for binding to the MAPKs ERK1 and ERK2.The Journal of biological chemistry · 2017Article
- The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.Journal of the American Chemical Society · 2016Article
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3 authors.
Funding
Abstract
The stabilities of 66 sequence variants of the human Pin1 WW domain have been determined by equilibrium thermal denaturation experiments. All 34 residues composing the hPin1 WW three-stranded beta-sheet structure could be replaced one at a time with at least one different natural or non-natural amino acid residue without leading to an unfolded protein. Alanine substitutions at only four positions within the hPin1 WW domain lead to a partially or completely unfolded protein-in the absence of a physiological ligand. The side chains of these four residues form a conserved, partially solvent-inaccessible, continuous hydrophobic minicore comprising the N- and C-termini. Ala mutations at five other residues, three of which constitute the ligand binding patch on the concave side of the beta-sheet, significantly destabilize the hPin1 WW domain without leading to an unfolded protein. The remaining mutations affect protein stability only slightly, suggesting that only a small subset of side chain interactions within the hPin1 WW domain are mandatory for acquiring and maintaining a stable, cooperatively folded beta-sheet structure.
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