Most Interacting Residues

A Monte Carlo algorithm is used to simulate the early steps of protein folding on a (2,1,0) lattice. An amino acid is randomly selected and displaced to a new available position on the lattice. The energy of both initial and final conformations is computed from the Miyazawa and Jernigan potential of mean force and the Metropolis criterion is then applied. The starting point is the protein structure in a random coil conformation and the simulation is typically of 10⁶ Monte Carlo steps. Output data may be smoothed using a method based on Pascal's Triangle and analysis of hydrophobic residues.

Analysis

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2) Optional: Email Notification for New Analysis
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Sample Query

To quickly see MIR analysis in action, try 1ASU.

Usage

SPROUTS allows the analysis of data from either a PDB entry or a FASTA file. When data is already available, you will be taken to the results immediately.

In the case that MIR data does not already exist, providing an email address allows us to notify you when analysis has completed.

Also see the MIR FAQ.

Please Cite

Protein intrachain contact prediction with most interacting residues (MIR). R Acuña, Z Lacroix, N Papandreou, and J Chomilier. Bio-Algorithms and Med-Systems 10 (4), 227-242.