ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural plasticity of 4-α-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Heptad insertion extends theBiodesign research · 2026Article
- Transition transferases prime bacterial capsule polymerization.Nature chemical biology · 2025Article
- The Curious Case of A31P, a Topology-Switching Mutant of the Repressor of Primer Protein: A Molecular Dynamics Study of Its Folding and Misfolding.Journal of chemical information and modeling · 2024Article
- Design and Selection of Heterodimerizing Helical Hairpins for Synthetic Biology.ACS synthetic biology · 2023Article
- Redirecting RiPP Biosynthetic Enzymes to Proteins and Backbone-Modified Substrates.ACS central science · 2022Article
- Structure and Thermal Stability of wtRop and RM6 Proteins through All-Atom Molecular Dynamics Simulations and Experiments.International journal of molecular sciences · 2021Article
- α-Helices in the Type III Secretion Effectors: A Prevalent Feature with Versatile Roles.International journal of molecular sciences · 2021Review
- Probing Protein Folding with Sequence-Reversed α-Helical Bundles.International journal of molecular sciences · 2021Article
- FerA is a Membrane-Associating Four-Helix Bundle Domain in the Ferlin Family of Membrane-Fusion Proteins.Scientific reports · 2018Article
- De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Expression, purification and crystallization of a protein resulting from the inversion of the amino-acid sequence of a helical bundle.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Structural plasticity of helical nanotubes based on coiled-coil assemblies.Structure (London, England : 1993) · 2015Article
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8 authors.
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Abstract
The dimeric Repressor of Primer (Rop) protein, a widely used model system for the study of coiled-coil 4-α-helical bundles, is characterized by a remarkable structural plasticity. Loop region mutations lead to a wide range of topologies, folding states, and altered physicochemical properties. A protein-folding study of Rop and several loop variants has identified specific residues and sequences that are linked to the observed structural plasticity. Apart from the native state, native-like and molten-globule states have been identified; these states are sensitive to reducing agents due to the formation of nonnative disulfide bridges. Pro residues in the loop are critical for the establishment of new topologies and molten globule states; their effects, however, can be in part compensated by Gly residues. The extreme plasticity in the assembly of 4-α-helical bundles reflects the capacity of the Rop sequence to combine a specific set of hydrophobic residues into strikingly different hydrophobic cores. These cores include highly hydrated ones that are consistent with the formation of interchain, nonnative disulfide bridges and the establishment of molten globules. Potential applications of this structural plasticity are among others in the engineering of bio-inspired materials.
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