From organ anatomy to atomic coordinates.

Understanding Brugada syndrome requires bridging five distinct orders of magnitude. The electrical defect begins at a sub-angstrom chemical bond, alters a twenty-nanometer channel inside a living membrane bilayer, slows conduction across millimeter tissue strands, and manifests as a lethal arrhythmia in the right ventricular outflow tract.

Here is the complete visual record of simulations, 3D anatomical meshes, and biophysical trajectories produced across this investigation. Click any figure to inspect the full-resolution uncompressed image.

All Scales (10)Organ & RVOT (30 mm)Tissue Electrophysiology1.4M-Atom Bilayer (20 nm)Atomic Hinge & Filter (3 Å)

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Organ Scale (0 to 30 mm)Voxel grid: 0-30 mm X, 0-30 mm Y, 0-25 mm Z

3D Biventricular Coordinate Field

A voxelized point-cloud reconstruction of human ventricular anatomy in explicit coordinate space. The rainbow colorbar maps coordinate depth across orthogonal projection planes.

Biventricular cardiac coordinate volume reconstructed for anatomical finite-element electrophysiology simulations.

Source: Anatomical coordinate model, 2026.

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Organ Scale (30 mm)Three orthogonal planes (x-y, x-z, y-z)

Right Ventricular Outflow Tract (RVOT) Localization

Three orthogonal cross-sections through the biventricular cardiac volume, highlighting the Right Ventricular Outflow Tract (RVOT) in solid red against the myocardial mesh. This identifies the primary anatomical seat of the Brugada ECG pattern.

Highlights the anatomical subregion responsible for the characteristic coved-type ST-segment elevation in leads V1-V2.

Source: 3D Outflow Tract Localization Screen, 2026.

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Tissue Scale (1 to 10 mm)Phase boundary parameter space

RVOT Conduction Threshold Phase Map

Bifurcation phase diagram illustrating the mathematical boundary between uniform wavefront conduction, conduction slowing, and functional electrical block across the RVOT epicardial wall.

Two-dimensional parameter sweep evaluating conduction safety margins under reduced peak sodium conductance and elevated tissue resistance.

Source: Paper 4 / RVOT Threshold Analysis (brugada.net/papers).

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Tissue Scale (1 mm to 100 µm)2D finite-difference tissue grid

2D Myocardial Wavefront Propagation Screen

Planar wavefront velocity and conduction curvature simulated across a 2D sheet of human ventricular myocytes at wild-type (100%), heterozygous loss (68.3%), and severe loss (31.3%) peak sodium current.

Evaluates the critical current threshold required to sustain electrical propagation across branching myocardial tissue strands.

Source: Paper 5 / 2D Expansion Screen (brugada.net/papers).

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Cellular Scale (-90 to -60 mV)Voltage-clamp steady-state curve

Resting Potential vs. Sodium Availability

Steady-state fast inactivation curve of human Nav1.5 showing how small depolarizations in resting membrane potential drastically reduce available sodium channels before the beat begins.

Demonstrates the steep voltage dependence of channel availability near typical resting potentials (-85 mV to -75 mV).

Source: Electrophysiology parameter calibration, 2026.

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Macromolecular Scale (20 nm)1,411,438 explicit atoms (POPC bilayer, 150 mM KCl)

1.41-Million-Atom Bilayer Cross Section

Full-length 2,016-residue human Nav1.5 embedded in a 643-lipid POPC membrane bilayer, solvated with 293,855 TIP4P/2005 water molecules, beta-1 auxiliary subunit, and N-terminal GFP fusion. Rendered in UCSF ChimeraX.

All-atom explicit solvent molecular dynamics system equilibrated under semi-isotropic Monte Carlo barostat at 310.15 K and 1 atm.

Source: Atomistic production trajectory, 2026 (brugada.net/gfp).

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Macromolecular Scale (10 to 20 nm)Bilayer thickness: 37.2 Å, 0.637 nm²/lipid

POPC Membrane Bilayer Side-View

Transmembrane profile of Nav1.5 illustrating the extracellular selectivity funnel, the four voltage-sensing domains, and the cytoplasmic N-terminal domain relative to the lipid headgroups.

Equilibrated lipid packing and bilayer dimensions matching experimental mammalian cardiac plasma membrane benchmarks.

Source: CHARMM36m bilayer equilibration, 2026.

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Atomic Scale (1 to 5 Å)Distance time series (ps vs. Å)

Position 104 Molecular Staple Time Series

Direct atom-pair distance between residue 104 and Asp84. In Wild-Type, Arg104 forms a rigid bidentate salt bridge clamp (3.4 Å). In R104Q, the loss of positive charge turns it into an unpartnered monodentate pivot that repeatedly unhinges into solvent.

Trajectory sampling demonstrating that substitution of neutral glutamine destabilizes the local cytoplasmic clamp without collapsing the pore.

Source: Production trajectory sampling, 2026 (brugada.net/gfp).

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Atomic Scale (5.2 to 5.4 Å, 12-15 Waters)Pore radius (Å) and water count

DEKA Pore Filter Radius and Hydration

The canonical selectivity filter radius (Asp372, Glu898, Lys1419, Ala1711) remains open at 5.2-5.4 Å (cryo-EM open state benchmark: 5.46 Å, PDB 6LQA) with continuous aqueous hydration (12-15 waters), disproving pore collapse.

Demonstrates that N-terminal GFP fusion does not induce allosteric filter constriction or hydrophobic dewetting.

Source: Production trajectory sampling, 2026 (brugada.net/gfp).

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Atomic Scale (1 to 5 Å RMSD)C-alpha RMSD across 2,016 residues

Domain Mobility vs. Core Stability

The transmembrane core backbone remains stable (RMSD ~3.5 Å), while the N-terminal cytoplasmic domain unhinges (1.35 Å to 4.2 Å), demonstrating localized structural loosening.

Root-mean-square deviation time series confirming that conformational drift is isolated to the cytoplasmic periphery.

Source: Production trajectory sampling, 2026 (brugada.net/gfp).