ArticleProceedings of the National Academy of Sciences of the United States of America2014
Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- The importance of input sequence set to consensus-derived proteins and their relationship to reconstructed ancestral proteins.Protein science : a publication of the Protein Society · 2024Article
- DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.Molecules (Basel, Switzerland) · 2022Review
- The folding and unfolding behavior of ribonuclease H on the ribosome.The Journal of biological chemistry · 2020Article
- Article
- The burst-phase folding intermediate of ribonuclease H changes conformation over evolutionary history.Biopolymers · 2018Article
- Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Non-native structure appears in microseconds during the folding of E. coli RNase H.Journal of molecular biology · 2015Article
- Autonomously folding protein fragments reveal differences in the energy landscapes of homologous RNases H.PloS one · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The molten globule, a conformational ensemble with significant secondary structure but only loosely packed tertiary structure, has been suggested to be a ubiquitous intermediate in protein folding. However, it is difficult to assess the tertiary packing of transiently populated species to evaluate this hypothesis. Escherichia coli RNase H is known to populate an intermediate before the rate-limiting barrier to folding that has long been thought to be a molten globule. We investigated this hypothesis by making mimics of the intermediate that are the ground-state conformation at equilibrium, using two approaches: a truncation to generate a fragment mimic of the intermediate, and selective destabilization of the native state using point mutations. Spectroscopic characterization and the response of the mimics to further mutation are consistent with studies on the transient kinetic intermediate, indicating that they model the early intermediate. Both mimics fold cooperatively and exhibit NMR spectra indicative of a closely packed conformation, in contrast to the hypothesis of molten tertiary packing. This result is important for understanding the nature of the subsequent rate-limiting barrier to folding and has implications for the assumption that many other proteins populate molten globule folding intermediates.
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