ArticleThe Journal of biological chemistry2010
Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 39 citations in OpenAlex.
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Reconstruction of ARNT PAS-B Unfolding Pathways by Steered Molecular Dynamics and Artificial Neural Networks.Journal of chemical theory and computation · 2021Article
- Modulation of a protein-folding landscape revealed by AFM-based force spectroscopy notwithstanding instrumental limitations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- Single-molecule Force Spectroscopy Reveals the Calcium Dependence of the Alternative Conformations in the Native State of a βγ-Crystallin Protein.The Journal of biological chemistry · 2016Article
- Chaperones rescue luciferase folding by separating its domains.The Journal of biological chemistry · 2014Article
- Improving single molecule force spectroscopy through automated real-time data collection and quantification of experimental conditions.Ultramicroscopy · 2014Article
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Sequential unfolding of beta helical protein by single-molecule atomic force microscopy.PloS one · 2013Article
- Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin.PLoS computational biology · 2013Article
- Identical RNA-protein interactions in vivo and in vitro and a scheme of folding the newly synthesized proteins by ribosomes.The Journal of biological chemistry · 2012Article
- Mutation of conserved histidines alters tertiary structure and nanomechanics of consensus ankyrin repeats.The Journal of biological chemistry · 2012Article
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
During co-translational folding, the nascent polypeptide chain is extruded sequentially from the ribosome exit tunnel and is [corrected] under severe conformational constraints [corrected] dictated by the one-dimensional geometry of the tunnel. [corrected] How do such vectorial constraints impact the folding pathway? Here, we combine single-molecule atomic force spectroscopy and steered molecular dynamics simulations to examine protein folding in the presence of one-dimensional constraints that are similar to those imposed on the nascent polypeptide chain. The simulations exquisitely reproduced the experimental unfolding and refolding force extension relationships and led to the full reconstruction of the vectorial folding pathway of a large polypeptide, the 253-residue consensus ankyrin repeat protein, NI6C. We show that fully stretched and then relaxed NI6C starts folding by the formation of local secondary structures, followed by the nucleation of three N-terminal repeats. This rate-limiting step is then followed by the vectorial and sequential folding of the remaining repeats. However, after partial unfolding, when allowed to refold, the C-terminal repeats successively regain structures without any nucleation step by using the intact N-terminal repeats as a template. These results suggest a pathway for the co-translational folding of repeat proteins and have implications for mechanotransduction.
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