ArticleProtein science : a publication of the Protein Society2016
Evolution of a protein folding nucleus.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed.
- PSSNet-An Accurate Super-Secondary Structure for Protein Segmentation.International journal of molecular sciences · 2022Article
- 3β-Corner Stability by Comparative Molecular Dynamics Simulations.International journal of molecular sciences · 2022Article
- Decoding an Amino Acid Sequence to Extract Information on Protein Folding.Molecules (Basel, Switzerland) · 2022Review
- Functionalization of a symmetric protein scaffold: Redundant folding nuclei and alternative oligomeric folding pathways.Protein science : a publication of the Protein Society · 2022Article
- Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function.Frontiers in molecular biosciences · 2022Article
- The ubiquitous buried water in the beta-trefoil architecture contributes to the folding nucleus and ~20% of the folding enthalpy.Protein science : a publication of the Protein Society · 2021Article
- Fold Evolution before LUCA: Common Ancestry of SH3 Domains and OB Domains.Molecular biology and evolution · 2021Article
- Cooperative hydrophobic core interactions in the β-trefoil architecture.Protein science : a publication of the Protein Society · 2021Article
- Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein.Protein science : a publication of the Protein Society · 2020Article
- Oligomerization of a symmetric β-trefoil protein in response to folding nucleus perturbation.Protein science : a publication of the Protein Society · 2020Article
- Ab initio folding of a trefoil-fold motif reveals structural similarity with a β-propeller blade motif.Protein science : a publication of the Protein Society · 2020Article
- Article
- Investigating the dynamics and polyanion binding sites of fibroblast growth factor-1 using hydrogen-deuterium exchange mass spectrometry.Protein science : a publication of the Protein Society · 2018Article
- Computational design of a symmetrical β-trefoil lectin with cancer cell binding activity.Scientific reports · 2017Article
- Crystal structure of MytiLec, a galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types.Scientific reports · 2016Article
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4 authors.
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Abstract
The folding nucleus (FN) is a cryptic element within protein primary structure that enables an efficient folding pathway and is the postulated heritable element in the evolution of protein architecture; however, almost nothing is known regarding how the FN structurally changes as complex protein architecture evolves from simpler peptide motifs. We report characterization of the FN of a designed purely symmetric β-trefoil protein by ϕ-value analysis. We compare the structure and folding properties of key foldable intermediates along the evolutionary trajectory of the β-trefoil. The results show structural acquisition of the FN during gene fusion events, incorporating novel turn structure created by gene fusion. Furthermore, the FN is adjusted by circular permutation in response to destabilizing functional mutation. FN plasticity by way of circular permutation is made possible by the intrinsic C3 cyclic symmetry of the β-trefoil architecture, identifying a possible selective advantage that helps explain the prevalence of cyclic structural symmetry in the proteome.
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