ArticleThe journal of physical chemistry letters2021
A Proposed Mechanism for the Initial Myosin Binding Event on the Cardiac Thin Filament: A Metadynamics Study.
Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 11 citations in OpenAlex.
- The Structural Role of Tropomyosin in Regulating Thin Filament Activation of Actin-Myosin Interaction.Sub-cellular biochemistry · 2026Review
- Unraveling Mutation-Induced Protein Communication Pathways in the Actomyosin Complex: Insights from Comprehensive Metadynamics Simulations.The journal of physical chemistry. B · 2025Article
- The transmission of mutation effects in a multiprotein machine: A comprehensive metadynamics study of the cardiac thin filament.Protein science : a publication of the Protein Society · 2024Article
- Human cardiac β-myosin powerstroke energetics: Thin filament, Pi displacement, and mutation effects.Biophysical journal · 2024Article
- Myosin's powerstroke transitions define atomic scale movement of cardiac thin filament tropomyosin.The Journal of general physiology · 2024Article
- Troponin-I-induced tropomyosin pivoting defines thin-filament function in relaxed and active muscle.The Journal of general physiology · 2023Article
- Multi-scale modeling will unravel connections between sarcomeric mutations and cardiomyopathies.Journal of molecular and cellular cardiology plus · 2023Article
- Myosin loop-4 is critical for optimal tropomyosin repositioning on actin during muscle activation and relaxation.The Journal of general physiology · 2023Article
- De Novo Asp219Val Mutation in Cardiac Tropomyosin Associated with Hypertrophic Cardiomyopathy.International journal of molecular sciences · 2022Article
- Structure and Dynamics of the Flexible Cardiac Troponin T Linker Domain in a Fully Reconstituted Thin Filament.Biochemistry · 2022Article
- Free-Energy Surfaces of Two Cardiac Thin Filament Conformational Changes during Muscle Contraction.The journal of physical chemistry. B · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The movement of tropomyosin over filamentous actin regulates the cross-bridge cycle of the thick with thin filament of cardiac muscle by blocking and revealing myosin binding sites. Tropomyosin exists in three, distinct equilibrium states with one state blocking myosin-actin interactions (blocked position) and the remaining two allowing for weak (closed position) and strong myosin binding (open position). However, experimental information illuminating how myosin binds to the thin filament and influences tropomyosin's transition across the actin surface is lacking. Using metadynamics, we mimic the effect of a single myosin head binding by determining the work required to pull small segments of tropomyosin toward the open position in several distinct regions of the thin filament. We find differences in required work due to the influence of cardiac troponin T lead to preferential binding sites and determine the mechanism of further myosin head recruitment.
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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.