ArticleJournal of molecular biology2008
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Resolving the fine structure in the energy landscapes of repeat proteins.QRB discovery · 2022Article
- Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold.Scientific reports · 2019Article
- Folding cooperativity and allosteric function in the tandem-repeat protein class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Context-Dependent Energetics of Loop Extensions in a Family of Tandem-Repeat Proteins.Biophysical journal · 2018Article
- High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.Journal of molecular biology · 2018Article
- Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution.Scientific reports · 2017Article
- Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics.Protein science : a publication of the Protein Society · 2017Article
- Protein knotting through concatenation significantly reduces folding stability.Scientific reports · 2016Article
- Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.Journal of molecular biology · 2016Article
- Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Biophysical journal · 2015Article
- Intermediates in the folding equilibrium of repeat proteins from the TPR family.European biophysics journal : EBJ · 2014Article
- Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.Protein science : a publication of the Protein Society · 2012Article
- Modulating repeat protein stability: the effect of individual helix stability on the collective behavior of the ensemble.Protein science : a publication of the Protein Society · 2011Article
- Calorimetric study of a series of designed repeat proteins: modular structure and modular folding.Protein science : a publication of the Protein Society · 2011Article
- Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Characterization of the unfolded state of repeat proteins.HFSP journal · 2008Article
- Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state.Journal of molecular biology · 2008Article
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Authors and funding
3 authors.
Funding
Abstract
Repeat proteins contain tandem arrays of a simple structural motif. In contrast to globular proteins, repeat proteins are stabilized only by interactions between residues that are relatively close together in the sequence, with no "long-range" interactions. Our work focuses on the tetratricopeptide repeat (TPR), a 34 amino acid helix-turn-helix motif found in tandem arrays in many natural proteins. Earlier, we reported the design and characterization of a series of consensus TPR (CTPR) proteins, which are built as arrays of multiple tandem copies of a 34 amino acid consensus sequence. Here, we present the results of extensive hydrogen exchange (HX) studies of the folding-unfolding behavior of two CTPR proteins (CTPR2 and CTPR3). We used HX to detect and characterize partially folded species that are populated at low frequency in the nominally folded state. We show that for both proteins the equilibrium folding-unfolding transition is non-two-state, but sequential, with the outermost helices showing a significantly higher probability than inner helices of being unfolded. We show that the experimentally observed unfolding behavior is consistent with the predictions of a simple Ising model, in which individual helices are treated as "spin-equivalents". The results that we present have general implications for our understanding of the thermodynamic properties of repeat proteins.
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