ArticleJournal of molecular biology2007
NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Shotgun scanning glycomutagenesis: A simple and efficient strategy for constructing and characterizing neoglycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Extreme Nonuniform Sampling for Protein NMR Dynamics Studies in Minimal Time.Journal of the American Chemical Society · 2019Article
- Folding while bound to chaperones.Current opinion in structural biology · 2018Review
- A molecular mechanism of chaperone-client recognition.Science advances · 2016Article
- Forces Driving Chaperone Action.Cell · 2016Article
- Substrate protein folds while it is bound to the ATP-independent chaperone Spy.Nature structural & molecular biology · 2016Article
- Using hydroxyl radical footprinting to explore the free energy landscape of protein folding.Methods (San Diego, Calif.) · 2015Article
- Network representation of conformational transitions between hidden intermediates of Rd-apocytochrome b562.The Journal of chemical physics · 2015Article
- Native contact density and nonnative hydrophobic effects in the folding of bacterial immunity proteins.PLoS computational biology · 2015Article
- Conformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7.Protein science : a publication of the Protein Society · 2013Article
- Cold denaturation of a protein dimer monitored at atomic resolution.Nature chemical biology · 2013Article
- Transiently populated intermediate functions as a branching point of the FF domain folding pathway.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Conformational properties of the unfolded state of Im7 in nondenaturing conditions.Journal of molecular biology · 2012Article
- The effect of C-terminal helix on the stability of FF domain studied by molecular dynamics simulation.International journal of molecular sciences · 2012Article
- Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.Journal of biomolecular NMR · 2011Article
- Dissecting key residues in folding and stability of the bacterial immunity protein 7.Protein engineering, design & selection : PEDS · 2011Article
- Malleability of folding intermediates in the homeodomain superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
- A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins.Journal of the American Chemical Society · 2010Article
- Single-molecule studies of the Im7 folding landscape.Journal of molecular biology · 2010Article
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5 authors.
Funding
Abstract
Previous work shows that the transiently populated, on-pathway intermediate in Im7 folding contains three of the four native alpha-helices docked around a core stabilised by native and non-native interactions. To determine the structure and dynamic properties of this species in more detail, we have used protein engineering to trap the intermediate at equilibrium and analysed the resulting proteins using NMR spectroscopy and small angle X-ray scattering. Four variants were created. In L53AI54A, two hydrophobic residues within helix III are truncated, preventing helix III from docking stably onto the developing hydrophobic core. In two other variants, the six residues encompassing the native helix III were replaced with three (H3G3) or six (H3G6) glycine residues. In the fourth variant, YY, two native tyrosine residues (Tyr55 and Tyr56) were re-introduced into H3G6 to examine their role in determining the properties of the intermediate ensemble. All four variants show variable peak intensities and broad peak widths, consistent with these proteins being conformationally dynamic. Chemical shift analyses demonstrated that L53AI54A and YY contain native-like secondary structure in helices I and IV, while helix II is partly formed and helix III is absent. Lack of NOEs and rapid NH exchange for L53AI54A, combined with detailed analysis of the backbone dynamics, indicated that the hydrophobic core of this variant is not uniquely structured, but fluctuates on the NMR timescale. The results demonstrate that though much of the native-like secondary structure of Im7 is present in the variants, their hydrophobic cores remain relatively fluid. The comparison of H3G3/H3G6 and L53AI54A/YY suggests that Tyr55 and/or Tyr56 interact with the three-helix core, leading other residues in this region of the protein to dock with the core as folding progresses. In this respect, the three-helix bundle acts as a template for formation of helix III and the creation of the native fold.
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