ArticleEMBO reports2005
The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments.
Article in EMBO reports, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 85 citations in OpenAlex.
- Force-Induced Ankle Opening Reveals Mechanical Stabilization of the Ankle of Human β-Cardiac Myosin.ACS nano · 2026Article
- Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026Article
- Optimal Sacrificial Domains in Mechanical Polyproteins:JACS Au · 2022Article
- Correlating single-molecule rupture mechanics with cell population adhesion by yeast display.Biophysical reports · 2022Article
- Neuromechanobiology: An Expanding Field Driven by the Force of Greater Focus.Advanced healthcare materials · 2021Review
- Interplay between Viscoelasticity and Force Rate Affects Sequential Unfolding in Polyproteins Pulled at Constant Velocity.Macromolecules · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Multiplexed protein force spectroscopy reveals equilibrium protein folding dynamics and the low-force response of von Willebrand factor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Single-molecule force spectroscopy reveals folding steps associated with hormone binding and activation of the glucocorticoid receptor.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins.Nature communications · 2015Article
- Connecting thermal and mechanical protein (un)folding landscapes.Biophysical journal · 2014Article
- Isopeptide bonds mechanically stabilize spy0128 in bacterial pili.Biophysical journal · 2013Article
- Early events in helix unfolding under external forces: a milestoning analysis.The journal of physical chemistry. B · 2012Article
- Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation.Biophysical journal · 2012Article
- Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy.Biophysical journal · 2011Article
- Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Calcium modulates force sensing by the von Willebrand factor A2 domain.Nature communications · 2011Article
- Real Time FRET Based Detection of Mechanical Stress in Cytoskeletal and Extracellular Matrix Proteins.Cellular and molecular bioengineering · 2011Article
- Fast and forceful refolding of stretched alpha-helical solenoid proteins.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The F-actin crosslinker filamin from Dictyostelium discoideum (ddFLN) has a rod domain consisting of six structurally similar immunoglobulin domains. When subjected to a stretching force, domain 4 unfolds at a lower force than all the other domains in the chain. Moreover, this domain shows a stable intermediate along its mechanical unfolding pathway. We have developed a mechanical single-molecule analogue to a double-jump stopped-flow experiment to investigate the folding kinetics and pathway of this domain. We show that an obligatory and productive intermediate also occurs on the folding pathway of the domain. Identical mechanical properties suggest that the unfolding and refolding intermediates are closely related. The folding process can be divided into two consecutive steps: in the first step 60 C-terminal amino acids form an intermediate at the rate of 55 s(-1); and in the second step the remaining 40 amino acids are packed on this core at the rate of 179 s(-1). This division increases the overall folding rate of this domain by a factor of ten compared with all other homologous domains of ddFLN that lack the folding intermediate.
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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.