ArticleProtein science : a publication of the Protein Society2012
Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.
Article in Protein science : a publication of the Protein Society, 2012. 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.
- A novel tetratricopeptide-repeat protein, TTP1, forms complexes with glutamyl-tRNA reductase and protochlorophyllide oxidoreductase during tetrapyrrole biosynthesis.Journal of experimental botany · 2024Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Engineering and exploiting synthetic allostery of NanoLuc luciferase.Nature communications · 2022Article
- Exploring the binding of rationally engineered tandem-repeat proteins to E3 ubiquitin ligase Keap1.Protein engineering, design & selection : PEDS · 2021Article
- Testing the length limit of loop grafting in a helical repeat protein.Current research in structural biology · 2021Article
- Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold.Scientific reports · 2019Article
- Exploring new strategies for grafting binding peptides onto protein loops using a consensus-designed tetratricopeptide repeat scaffold.Protein science : a publication of the Protein Society · 2019Article
- Context-Dependent Energetics of Loop Extensions in a Family of Tandem-Repeat Proteins.Biophysical journal · 2018Article
- Removal of a consensus proline is not sufficient to allow tetratricopeptide repeat oligomerization.Protein science : a publication of the Protein Society · 2017Article
- A method for rapid high-throughput biophysical analysis of proteins.Scientific reports · 2017Article
- Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.Journal of molecular biology · 2016Article
- Article
- Intermediates in the folding equilibrium of repeat proteins from the TPR family.European biophysics journal : EBJ · 2014Article
- LcrH, a class II chaperone from the type three secretion system, has a highly flexible native structure.The Journal of biological chemistry · 2013Article
- Investigation of effects of terpene skin penetration enhancers on stability and biological activity of lysozyme.AAPS PharmSciTech · 2012Article
- Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Tetratricopeptide repeats (TPRs) are a class of all alpha-helical repeat proteins that are comprised of 34-aa helix-turn-helix motifs. These stack together to form nonglobular structures that are stabilized by short-range interactions from residues close in primary sequence. Unlike globular proteins, they have few, if any, long-range nonlocal stabilizing interactions. Several studies on designed TPR proteins have shown that this modular structure is reflected in their folding, that is, modular multistate folding is observed as opposed to two-state folding. Here we show that TPR multistate folding can be suppressed to approximate two-state folding through modulation of intrinsic stability or extrinsic environmental variables. This modulation was investigated by comparing the thermodynamic unfolding under differing buffer regimes of two distinct series of consensus-designed TPR proteins, which possess different intrinsic stabilities. A total of nine proteins of differing sizes and differing consensus TPR motifs were each thermally and chemically denatured and their unfolding monitored using differential scanning calorimetry (DSC) and CD/fluorescence, respectively. Analyses of both the DSC and chemical denaturation data show that reducing the total stability of each protein and repeat units leads to observable two-state unfolding. These data highlight the intimate link between global and intrinsic repeat stability that governs whether folding proceeds by an observably two-state mechanism, or whether partial unfolding yields stable intermediate structures which retain sufficient stability to be populated at equilibrium.
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