ArticleJournal of molecular biology2007
The folding pathway of T4 lysozyme: an on-pathway hidden folding intermediate.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Protein structure and folding pathway prediction based on remote homologs recognition using PAthreader.Communications biology · 2023Article
- Prediction and Validation of a Protein's Free Energy Surface Using Hydrogen Exchange and (Importantly) Its Denaturant Dependence.Journal of chemical theory and computation · 2022Article
- DEER-PREdict: Software for efficient calculation of spin-labeling EPR and NMR data from conformational ensembles.PLoS computational biology · 2021Article
- The Non-dominant AAA+ Ring in the ClpAP Protease Functions as an Anti-stalling Motor to Accelerate Protein Unfolding and Translocation.Cell reports · 2020Article
- How internal cavities destabilize a protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity.Biophysical journal · 2016Article
- Start2Fold: a database of hydrogen/deuterium exchange data on protein folding and stability.Nucleic acids research · 2016Article
- Network representation of conformational transitions between hidden intermediates of Rd-apocytochrome b562.The Journal of chemical physics · 2015Article
- Folding of a large protein at high structural resolution.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modulation of a protein free-energy landscape by circular permutation.The journal of physical chemistry. B · 2013Article
- 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
- Lessons from the lysozyme of phage T4.Protein science : a publication of the Protein Society · 2010Review
- A single mutation at residue 25 populates the folding intermediate of E. coli RNase H and reveals a highly dynamic partially folded ensemble.Journal of molecular biology · 2009Article
- Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape.Protein science : a publication of the Protein Society · 2009Article
- Subdomain competition, cooperativity, and topological frustration in the folding of CheY.Journal of molecular biology · 2008Article
- Kinetic barriers and the role of topology in protein and RNA folding.Protein science : a publication of the Protein Society · 2008Review
- Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: evidence for a kinetic partitioning mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Protein folding and misfolding: mechanism and principles.Quarterly reviews of biophysics · 2007Review
- Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway.Protein science : a publication of the Protein Society · 2007Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
T4 lysozyme has two easily distinguishable but energetically coupled domains: the N and C-terminal domains. In earlier studies, an amide hydrogen/deuterium exchange pulse-labeling experiment detected a stable submillisecond intermediate that accumulates before the rate-limiting transition state. It involves the formation of structures in both the N and C-terminal regions. However, a native-state hydrogen exchange experiment subsequently detected an equilibrium intermediate that only involves the formation of the C-terminal domain. Here, using stopped-flow circular dichroism and fluorescence, amide hydrogen exchange-folding competition, and protein engineering methods, we re-examined the folding pathway of T4-lysozyme. We found no evidence for the existence of a stable folding intermediate before the rate-limiting transition state at neutral pH. In addition, using native-state hydrogen exchange-directed protein engineering, we created a mimic of the equilibrium intermediate. We found that the intermediate mimic folds with the same rate as the wild-type protein, suggesting that the equilibrium intermediate is an on-pathway intermediate that exists after the rate-limiting transition state.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.