Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Long-timescale molecular dynamics simulations elucidate the dynamics and kinetics of exposure of the hydrophobic patch in troponin C.

Biophysical journal - 17 Oct 2012

Lindert Steffen, Kekenes-Huskey Peter M, McCammon J Andrew

Abstract excerpt

Troponin (Tn) is an important regulatory protein in the thin-filament complex of cardiomyocytes. Calcium binding to the troponin C (TnC) subunit causes a change in its dynamics that leads to the transient opening of a hydrophobic patch on TnC's surface, to which a helix of another subunit, troponin I (TnI), binds. This process initiates contraction, making it an important target for studies investigating the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Calcium
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Molecular Sequence Data

Share to Myocytes, Cardiac

Share to Protein Structure, Tertiary

Share to Troponin C

Source

Open in PubMed Open full text

Identifiers

PMID: 23083722
DOI: 10.1016/j.bpj.2012.08.058
PMCID: PMC3475331

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Long-timescale molecular dynamics simulations elucidate the dynamics and kinetics of exposure of the hydrophobic patch in troponin C.PMID 23083722Read ↗

Molecular Dynamics and Umbrella Sampling Simulations Elucidate Differences in Troponin C Isoform and Mutant Hydrophobic Patch Exposure.Semantic proximity Read ↗

Changes in the dynamics of the cardiac troponin C molecule explain the effects of Ca2+-sensitizing mutations.Semantic proximity Read ↗

Molecular basis of calcium-sensitizing and desensitizing mutations of the human cardiac troponin C regulatory domain: a multi-scale simulation study.Semantic proximity Read ↗

Umbrella Sampling Simulations of Cardiac Thin Filament Reveal Thermodynamic Consequences of Troponin I Inhibitory Peptide Mutations.Semantic proximity Read ↗

Computational Methods Elucidate Consequences of Mutations and Post-translational Modifications on Troponin I Effective Concentration to Troponin C.Semantic proximity Read ↗

Molecular Effects of cTnC DCM Mutations on Calcium Sensitivity and Myofilament Activation-An Integrated Multiscale Modeling Study.Semantic proximity Read ↗

Investigating cardiomyopathies with atomistic simulations of cardiac TroponinSemantic proximity Read ↗

Allosteric Transmission along a Loosely Structured Backbone Allows a Cardiac Troponin C Mutant to Function with Only One Ca2+ Ion.Semantic proximity Read ↗

Pathogenic peptide deviations support a model of adaptive evolution of chordate cardiac performance by troponin mutations.Semantic proximity Read ↗

Significance of troponin dynamics for Ca2+-mediated regulation of contraction and inherited cardiomyopathy.Semantic proximity Read ↗

Calcium Binding Affinity in the Mutational Landscape of Troponin-C: Free Energy Calculation, Coevolution Modeling and Machine LearningSemantic proximity Read ↗

Amide hydrogens reveal a temperature-dependent structural transition that enhances site-II Ca2+-binding affinity in a C-domain mutant of cardiac troponin C.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.