ArticleBiophysical journal2010
Mechanical unfolding of an ankyrin repeat protein.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Cooperative mechanics of PR65 scaffold underlies the allosteric regulation of the phosphatase PP2A.Structure (London, England : 1993) · 2023Article
- Snapshots of urea-induced early structural changes and unfolding of an ankyrin repeat protein at atomic resolution.Protein science : a publication of the Protein Society · 2022Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Resolving the fine structure in the energy landscapes of repeat proteins.QRB discovery · 2022Article
- Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold.Scientific reports · 2019Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- Context-Dependent Energetics of Loop Extensions in a Family of Tandem-Repeat Proteins.Biophysical journal · 2018Article
- Force regulated conformational change of integrin αMatrix biology : journal of the International Society for Matrix Biology · 2017Article
- Regulation of the transient receptor potential channel TRPA1 by its N-terminal ankyrin repeat domain.Journal of molecular modeling · 2013Article
- Distinct roles of TRP channels in auditory transduction and amplification in Drosophila.Neuron · 2013Article
- Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin.PLoS computational biology · 2013Article
- Mechanical properties of β-catenin revealed by single-molecule experiments.Biophysical journal · 2012Article
- Mutation of conserved histidines alters tertiary structure and nanomechanics of consensus ankyrin repeats.The Journal of biological chemistry · 2012Article
- Prying open single GroES ring complexes by force reveals cooperativity across domains.Biophysical journal · 2012Article
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
- Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Biophysical journal · 2011Article
- Extension of a three-helix bundle domain of myosin VI and key role of calmodulins.Biophysical journal · 2011Article
- Inhibitor binding increases the mechanical stability of staphylococcal nuclease.Biophysical journal · 2011Article
- Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.The Journal of biological chemistry · 2010Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ankryin repeat proteins comprise tandem arrays of a 33-residue, predominantly alpha-helical motif that stacks roughly linearly to produce elongated and superhelical structures. They function as scaffolds mediating a diverse range of protein-protein interactions, and some have been proposed to play a role in mechanical signal transduction processes in the cell. Here we use atomic force microscopy and molecular-dynamics simulations to investigate the natural 7-ankyrin repeat protein gankyrin. We find that gankyrin unfolds under force via multiple distinct pathways. The reactions do not proceed in a cooperative manner, nor do they always involve fully stepwise unfolding of one repeat at a time. The peeling away of half an ankyrin repeat, or one or more ankyrin repeats, occurs at low forces; however, intermediate species are formed that are resistant to high forces, and the simulations indicate that in some instances they are stabilized by nonnative interactions. The unfolding of individual ankyrin repeats generates a refolding force, a feature that may be more easily detected in these proteins than in globular proteins because the refolding of a repeat involves a short contraction distance and incurs a low entropic cost. We discuss the origins of the differences between the force- and chemical-induced unfolding pathways of ankyrin repeat proteins, as well as the differences between the mechanics of natural occurring ankyrin repeat proteins and those of designed consensus ankyin repeat and globular proteins.
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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.