ArticleJournal of molecular biology2009
The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Protein structure and folding pathway prediction based on remote homologs recognition using PAthreader.Communications biology · 2023Article
- Article
- The folding and unfolding behavior of ribonuclease H on the ribosome.The Journal of biological chemistry · 2020Article
- Article
- Kinetic and structural comparison of a protein's cotranslational folding and refolding pathways.Science advances · 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
- Article
- Non-native structure appears in microseconds during the folding of E. coli RNase H.Journal of molecular biology · 2015Article
- Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Early folding events protect aggregation-prone regions of a β-rich protein.Structure (London, England : 1993) · 2013Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- The H2A-H2B dimeric kinetic intermediate is stabilized by widespread hydrophobic burial with few fully native interactions.Journal of molecular biology · 2012Article
- Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Proteins can sample a variety of partially folded conformations during the transition between the unfolded and native states. Some proteins never significantly populate these high-energy states and fold by an apparently two-state process. However, many proteins populate detectable, partially folded forms during the folding process. The role of such intermediates is a matter of considerable debate. A single amino acid change can convert Escherichia coli ribonuclease H from a three-state folder that populates a kinetic intermediate to one that folds in an apparent two-state fashion. We have compared the folding trajectories of the three-state RNase H and the two-state RNase H, proteins with the same native-state topology but altered regional stability, using a protein engineering approach. Our data suggest that both versions of RNase H fold through a similar trajectory with similar high-energy conformations. Mutations in the core and the periphery of the protein affect similar aspects of folding for both variants, suggesting a common trajectory with folding of the core region followed by the folding of the periphery. Our results suggest that formation of specific partially folded conformations may be a general feature of protein folding that can promote, rather than hinder, efficient folding.
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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.