ArticleProtein science : a publication of the Protein Society2007
Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed.
- A high-sensitivity stopped-flow EPR system to monitor millisecond conformational kinetics in spin-labeled proteins.Protein science : a publication of the Protein Society · 2025Article
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.Protein science : a publication of the Protein Society · 2024Article
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.bioRxiv : the preprint server for biology · 2024Article
- Local Xenon-Protein Interaction Produces Global Conformational Change and Allosteric Inhibition in Lysozyme.Biochemistry · 2023Article
- How internal cavities destabilize a protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Modulating long-range energetics via helix stabilization: A case study using T4 lysozyme.Protein science : a publication of the Protein Society · 2018Article
- Equilibrium folding dynamics of meACP in water, heavy water, and low concentration of urea.Scientific reports · 2017Article
- Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.Biophysical journal · 2016Article
- Network representation of conformational transitions between hidden intermediates of Rd-apocytochrome b562.The Journal of chemical physics · 2015Article
- Role of cavities and hydration in the pressure unfolding of T4 lysozyme.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state.Biophysical journal · 2013Article
- Modulation of a protein free-energy landscape by circular permutation.The journal of physical chemistry. B · 2013Article
- The ribosome modulates nascent protein folding.Science (New York, N.Y.) · 2011Article
- High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Interaction energy based protein structure networks.Biophysical journal · 2010Article
- Resolving Conformational and Rotameric Exchange in Spin-Labeled Proteins Using Saturation Recovery EPR.Applied magnetic resonance · 2010Article
- Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Insights from coarse-grained Gō models for protein folding and dynamics.International journal of molecular sciences · 2009Review
- A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer.Journal of the American Chemical Society · 2008Article
- Subdomain competition, cooperativity, and topological frustration in the folding of CheY.Journal of molecular biology · 2008Article
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3 authors.
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Abstract
Intermediates along a protein's folding pathway can play an important role in its biology. Previous kinetics studies have revealed an early folding intermediate for T4 lysozyme, a small, well-characterized protein composed of an N-terminal and a C-terminal subdomain. Pulse-labeling hydrogen exchange studies suggest that residues from both subdomains contribute to the structure of this intermediate. On the other hand, equilibrium native state hydrogen experiments have revealed a high-energy, partially unfolded form of the protein that has an unstructured N-terminal subdomain and a structured C-terminal subdomain. To resolve this discrepancy between kinetics and equilibrium data, we performed detailed kinetics analyses of the folding and unfolding pathways of T4 lysozyme, as well as several point mutants and large-scale variants. The data support the argument for the presence of two distinct intermediates, one present on each side of the rate-limiting transition state barrier. The effects of circular permutation and site-specific mutations in the wild-type and circular permutant background, as well as a fragment containing just the C-terminal subdomain, support a model for the unfolding intermediate with an unfolded N-terminal and a folded C-terminal subdomain. Our results suggest that the partially unfolded form identified by native state hydrogen exchange resides on the folded side of the rate-limiting transition state and is, therefore, under most conditions, a "hidden" intermediate.
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