ArticleBiophysical journal2010
Fast and forceful refolding of stretched alpha-helical solenoid proteins.
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 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed.
- Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65.JACS Au · 2026Article
- Cooperative mechanics of PR65 scaffold underlies the allosteric regulation of the phosphatase PP2A.Structure (London, England : 1993) · 2023Article
- Unraveling the Mechanics of a Repeat-Protein Nanospring: From Folding of Individual Repeats to Fluctuations of the Superhelix.ACS nano · 2022Article
- Mechanical Stability of a Small, Highly-Luminescent Engineered Protein NanoLuc.International journal of molecular sciences · 2020Article
- A Region of UNC-89 (Obscurin) Lying between Two Protein Kinase Domains Is a Highly Elastic Spring Required for Proper Sarcomere Organization.Journal of molecular biology · 2020Article
- Cytoskeleton-inspired artificial protein design to enhance polymer network elasticity.Macromolecules · 2020Article
- Article
- Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.Biophysical journal · 2017Article
- Chaperones rescue luciferase folding by separating its domains.The Journal of biological chemistry · 2014Article
- Functional and genomic analyses of alpha-solenoid proteins.PloS one · 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
- Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation.Biophysical journal · 2012Article
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
- Mechanical unfolding studies of protein molecules.Biophysics (Nagoya-shi, Japan) · 2012Review
- Nanomechanics of streptavidin hubs for molecular materials.Advanced materials (Deerfield Beach, Fla.) · 2011Article
- Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Biophysical journal · 2011Article
- Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor.The Journal of biological chemistry · 2011Article
- Inhibitor binding increases the mechanical stability of staphylococcal nuclease.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
9 authors.
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Abstract
Anfinsen's thermodynamic hypothesis implies that proteins can encode for stretching through reversible loss of structure. However, large in vitro extensions of proteins that occur through a progressive unfolding of their domains typically dissipate a significant amount of energy, and therefore are not thermodynamically reversible. Some coiled-coil proteins have been found to stretch nearly reversibly, although their extension is typically limited to 2.5 times their folded length. Here, we report investigations on the mechanical properties of individual molecules of ankyrin-R, beta-catenin, and clathrin, which are representative examples of over 800 predicted human proteins composed of tightly packed alpha-helical repeats (termed ANK, ARM, or HEAT repeats, respectively) that form spiral-shaped protein domains. Using atomic force spectroscopy, we find that these polypeptides possess unprecedented stretch ratios on the order of 10-15, exceeding that of other proteins studied so far, and their extension and relaxation occurs with minimal energy dissipation. Their sequence-encoded elasticity is governed by stepwise unfolding of small repeats, which upon relaxation of the stretching force rapidly and forcefully refold, minimizing the hysteresis between the stretching and relaxing parts of the cycle. Thus, we identify a new class of proteins that behave as highly reversible nanosprings that have the potential to function as mechanosensors in cells and as building blocks in springy nanostructures. Our physical view of the protein component of cells as being comprised of predominantly inextensible structural elements under tension may need revision to incorporate springs.
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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.