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

1) Select analysis mode:

PDB ID(s): PDB ID(s)
Upload FASTA: Upload FASTA
PDB ID Analysis Mode:
PDB ID(s):
This must be comma separated and have no more than five IDs.
Custom Data Analysis Mode:
Retrieval Code:
Enter a 4-letter alphanumeric annotation to identify and retrieve your submission. May not be a PDB ID.
FASTA file:
ONE SEQUENCE ONLY, 1- letter AA format.

2) Optional: Email Notification for New Analysis

Email

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.