ArticleProceedings of the National Academy of Sciences of the United States of America2008
Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding.Molecules (Basel, Switzerland) · 2023Review
- Protein structure and folding pathway prediction based on remote homologs recognition using PAthreader.Communications biology · 2023Article
- Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion.The journal of physical chemistry. B · 2022Article
- Retrospective study for the universal applicability of the residue-based linear free energy relationship in the two-state exchange of protein molecules.Scientific reports · 2022Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.Molecules (Basel, Switzerland) · 2022Review
- Real-time tracking of protein unfolding with time-resolved x-ray solution scattering.Structural dynamics (Melville, N.Y.) · 2020Article
- Protein tertiary structure and the myoglobin phase diagram.Scientific reports · 2019Article
- Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.The journal of physical chemistry. B · 2018Article
- Exploring the Sequence-based Prediction of Folding Initiation Sites in Proteins.Scientific reports · 2017Article
- The case for defined protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.Accounts of chemical research · 2017Article
- Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- 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
- Crystal structure of group II intron domain 1 reveals a template for RNA assembly.Nature chemical biology · 2015Article
- Influence of reactive species on the modification of biomolecules generated from the soft plasma.Scientific reports · 2015Article
- Article
- Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Probing the non-native H helix translocation in apomyoglobin folding intermediates.Biochemistry · 2014Article
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7 authors.
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Abstract
The earliest steps in the folding of proteins are complete on an extremely rapid time scale that is difficult to access experimentally. We have used rapid-mixing quench-flow methods to extend the time resolution of folding studies on apomyoglobin and elucidate the structural and dynamic features of members of the ensemble of intermediate states that are populated on a submillisecond time scale during this process. The picture that emerges is of a continuum of rapidly interconverting states. Even after only 0.4 ms of refolding time a compact state is formed that contains major parts of the A, G, and H helices, which are sufficiently well folded to protect amides from exchange. The B, C, and E helix regions fold more slowly and fluctuate rapidly between open and closed states as they search docking sites on this core; the secondary structure in these regions becomes stabilized as the refolding time is increased from 0.4 to 6 ms. No further stabilization occurs in the A, G, H core at 6 ms of folding time. These studies begin to time-resolve a progression of compact states between the fully unfolded and native folded states and confirm the presence an ensemble of intermediates that interconvert in a hierarchical sequence as the protein searches conformational space on its folding trajectory.
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