ArticleProceedings of the National Academy of Sciences of the United States of America2018
The consequences of cavity creation on the folding landscape of a repeat protein depend upon context.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Stability and cooperativity in chimeric de novo TIM barrels via quarter swapping.Protein science : a publication of the Protein Society · 2026Article
- Adaptation of Folding and Function of a Nuclease from the Cold Deep Sea.Journal of molecular biology · 2026Article
- A molten globule ensemble primes Arf1-GDP for the nucleotide switch.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Response and adaptation of the transcriptional heat shock response to pressure.Frontiers in microbiology · 2024Article
- Pressure pushes tRNAProceedings of the National Academy of Sciences of the United States of America · 2023Article
- High Pressure CPMG and CEST Reveal That Cavity Position Dictates Distinct Dynamic Disorder in the PP32 Repeat Protein.The journal of physical chemistry. B · 2022Article
- Inline small-angle X-ray scattering-coupled chromatography under extreme hydrostatic pressure.Protein science : a publication of the Protein Society · 2022Article
- Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR.Biology · 2021Article
- Protein unfolded states populated at high and ambient pressure are similarly compact.Biophysical journal · 2021Article
- High-pressure small-angle X-ray scattering cell for biological solutions and soft materials.Journal of applied crystallography · 2021Article
- Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8.Communications biology · 2020Article
- A Second Backbone: The Contribution of a Buried Asparagine Ladder to the Global and Local Stability of a Leucine-Rich Repeat Protein.Biochemistry · 2019Article
- Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates.Biophysical journal · 2019Article
- Precision medicine review: rare driver mutations and their biophysical classification.Biophysical reviews · 2019Review
- Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018Review
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Authors and funding
13 authors.
Funding
Abstract
The effect of introducing internal cavities on protein native structure and global stability has been well documented, but the consequences of these packing defects on folding free-energy landscapes have received less attention. We investigated the effects of cavity creation on the folding landscape of the leucine-rich repeat protein pp32 by high-pressure (HP) and urea-dependent NMR and high-pressure small-angle X-ray scattering (HPSAXS). Despite a modest global energetic perturbation, cavity creation in the N-terminal capping motif (N-cap) resulted in very strong deviation from two-state unfolding behavior. In contrast, introduction of a cavity in the most stable, C-terminal half of pp32 led to highly concerted unfolding, presumably because the decrease in stability by the mutations attenuated the N- to C-terminal stability gradient present in WT pp32. Interestingly, enlarging the central cavity of the protein led to the population under pressure of a distinct intermediate in which the N-cap and repeats 1-4 were nearly completely unfolded, while the fifth repeat and the C-terminal capping motif remained fully folded. Thus, despite modest effects on global stability, introducing internal cavities can have starkly distinct repercussions on the conformational landscape of a protein, depending on their structural and energetic context.
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