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Molecular Dynamics Simulation Service

Protein–Protein / Small Molecule

High-precision molecular dynamics simulation for protein complexes and small molecule interactions. Evaluate complex stability, binding interface dynamics, and interaction mechanisms at atomic scale using in-house HPC infrastructure.

Zero Experimental Cost
Confidence-Scored Results
Publication-Ready Figures
Wet-Lab Validation Available
24h Scientific Support

Service Overview

ICDMO provides molecular dynamics (MD) simulation for protein complexes and protein–small molecule interactions. MD simulation uses 3D structures (PDB format) as initial models with classical force fields to describe atomic interactions, dynamically tracking atom trajectories to reveal binding and dissociation processes, interface rearrangement, conformational transitions, and key residue contributions to stability. Simulations are performed on in-house HPC servers for fast turnaround and fully reproducible results — all integrated with downstream experimental validation platforms (Y2H, Co-IP, SPR, MST, BLI, ITC).

Technical Advantages

High-Performance Computing
In-house HPC infrastructure delivers fast turnaround with fully reproducible simulations at any timescale.
Publication-Grade Visualizations
RMSD, RMSF, H-bond networks, and energy heatmaps formatted for top-tier journal submission.
Expert Team
Scientists with decades of combined MD experience covering proteins, nucleic acids, and small molecules.
Full Experimental Integration
Seamlessly validated with Y2H, Co-IP, SPR, MST, BLI, and ITC platforms.
Customizable Parameters
Temperature gradients (50–80°C), metal ions, membrane systems, and special force field setups.
Comprehensive Energy Analysis
MM/GBSA binding free energy with per-residue and per-ligand moiety decomposition.

Technical Principle

AMBER ff14SB force field is applied for protein atoms; AmberTools antechamber with AM1-BCC charges is used for small molecules. Systems are solvated in a TIP3P explicit water box (10 Å buffer), neutralized with Na⁺/Cl⁻ ions, and subjected to energy minimization → heating (0 K → 300 K, Langevin thermostat) → NPT density equilibration → unrestrained production MD (50–400 ns, trajectory output every 10 ps). Trajectory analysis uses cpptraj (AMBER) and VMD visualization.

Applications

Protein–Protein MD Simulation

Dynamic interaction mechanism capture across entire simulation timescale
Mutation & stability assessment — predict effect of point mutations on binding affinity
Experimental guidance: identify key residues for targeted mutagenesis or inhibitor design
Publication-quality structural visualizations of binding interface dynamics

Protein–Small Molecule MD Simulation

Binding mechanism analysis: pose stability, induced-fit effects, key pharmacophore contacts
Structure–activity relationship (SAR) studies and lead optimization
Experimental validation support: suggest optimal labeling/mutation sites for biophysical assays
Publication-ready RMSD, RMSF, H-bond occupancy, and 2D interaction diagrams

Trajectory Analysis Methods

1RMSD (Root Mean Square Deviation) — quantifies structural deviation from the reference frame over simulation time
2RMSF (Root Mean Square Fluctuation) — identifies flexible vs. stable regions at residue/atom level
3Hydrogen Bond Analysis — donor–acceptor distance (<3.5 Å), angle (<35°), bond counts, lifetimes, and spatial distribution
4MM/GBSA Binding Free Energy — van der Waals, electrostatic, and solvation contribution breakdown
5Per-residue energy decomposition — identifies dominant stabilizing/destabilizing residues
6B-factor analysis and conformational change mapping

Sample Requirements

1Protein–Protein: PDB file of docked complex + sequence information (≤800 aa total recommended)
2Protein–Ligand: 3D ligand structure (mol2 / sdf / pdb) + 2D chemical structural diagram
3Sequence-only submissions: require upstream AOS / molecular docking service prior to MD
4High-resolution, complete structures strongly preferred; partial structures evaluated case-by-case

Technical Workflow

1
Data Preparation & System Setup
Receive PDB structure. Assign force fields (AMBER ff14SB / AM1-BCC). Add hydrogens, solvate in TIP3P water box (10 Å), neutralize with Na⁺/Cl⁻.
2
Energy Minimization
Remove steric clashes and relax geometry using positional restraints on backbone. Optimize water/ions first. Up to 5,000 steps.
3
Heating (0 K → 300 K)
Gradually increase temperature using Langevin thermostat. Backbone restraints maintained. ~50,000 steps (2 fs timestep). Optional temperature gradient (50–80°C).
4
NPT Equilibration
Equilibrate under constant pressure (1 atm) and temperature (300 K). Gradually release backbone restraints over 100–200 ps.
5
Production MD Run
Unrestrained production MD for 50–400 ns. Trajectory snapshots output every 10 ps.
6
Trajectory Analysis & Reporting
cpptraj + VMD analysis: RMSD, RMSF, H-bonds, MM/GBSA free energy. Deliver publication-grade figures and comprehensive report.

Service Timeline & Deliverables

Simulation TimeTurnaroundDeliverables
100 ns production run~15 business daysTrajectory files (PDB/DCD), RMSD/RMSF plots, H-bond analysis, MM/GBSA binding free energy report, start vs. final structure comparison
200 ns production run~15 business daysAs above + extended conformational sampling, interaction stability profile
400 ns production run~15 business daysFull analysis suite + enhanced sampling statistics, detailed per-residue energy decomposition
Custom (metal ions, membrane, special setup)Quoted on requestCustom deliverables discussed at consultation

Service Process

1
Online Consultation
2
Solution Matching
3
Service Contract
4
AI Computation
5
Project Report

Note: All services are for research use only and not intended for diagnostic or therapeutic purposes.

Get a Custom Quote

Our scientific team responds within 24 hours with a detailed technical proposal and pricing tailored to your research goals.

Contact Us Online Consultation

Standard Deliverables

Detailed analysis report (PDF)
Raw data files & processed outputs
High-resolution publication figures
Interaction scoring tables (Excel)
Project summary presentation

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