ArticleBiophysical journal2007
Structural change and nucleotide dissociation of Myosin motor domain: dual go model simulation.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed.
- Building a macro-mixing dual-basin Gō model using the Multistate Bennett Acceptance Ratio.Biophysics and physicobiology · 2019Article
- Gō model revisited.Biophysics and physicobiology · 2019Review
- Effects of ATP and actin-filament binding on the dynamics of the myosin II S1 domain.Biophysical journal · 2013Article
- The mechanism of the converter domain rotation in the recovery stroke of myosin motor protein.Proteins · 2012Article
- Article
- Simulations of the alternating access mechanism of the sodium symporter Mhp1.Biophysical journal · 2011Article
- Drug export and allosteric coupling in a multidrug transporter revealed by molecular simulations.Nature communications · 2010Article
- Many local motions cooperate to produce the adenylate kinase conformational transition.Journal of molecular biology · 2010Article
- Entropic mechanism of large fluctuation in allosteric transition.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The energy profiles of atomic conformational transition intermediates of adenylate kinase.Proteins · 2009Article
- Insights from coarse-grained Gō models for protein folding and dynamics.International journal of molecular sciences · 2009Review
- Coevolution of function and the folding landscape: correlation with density of native contacts.Biophysical journal · 2008Article
- Energetics of subdomain movements and fluorescence probe solvation environment change in ATP-bound myosin.European biophysics journal : EBJ · 2008Article
- Src kinase conformational activation: thermodynamics, pathways, and mechanisms.PLoS computational biology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigated the structural relaxation of myosin motor domain from the pre-power stroke state to the near-rigor state using molecular dynamics simulation of a coarse-grained protein model. To describe the spontaneous structural change, we propose a dual Gō-model-a variant of the Gō-like model that has two reference structures. The nucleotide dissociation process is also studied by introducing a coarse-grained nucleotide in the simulation. We found that the myosin structural relaxation toward the near-rigor conformation cannot be completed before the nucleotide dissociation. Moreover, the relaxation and the dissociation occurred cooperatively when the nucleotide was tightly bound to the myosin head. The result suggested that the primary role of the nucleotide is to suppress the structural relaxation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.