1. Prediction of the Number of Residue Contacts in Proteins
발표자: 정 제 균
Fiero Fariselli and Rita Casadio
CIRB Biocomputing Unit and Lab. of Biophysics, Dept. Biology University of Bologna

2. Introduction The elucidation of the functional properties of protein
The process of protein folding
Three-dimensional structure
Residue contacts constrain protein folding and characterize different protein structure.
Knowing the correct positions of residue contacts in protein has been proven extremely useful to determine the three-dimensional structure.

3. 2D Protein Prediction: An Overview

4. Binary Version: Prediction of Contacts

6. Computation of Residue Solvent Accessibility and Contact Number
using the DSSP program (Kabsch and Sander 1983)
The value is normalized to the maximal exposed surface area of each residue (Rose et al., 1985).
The number of inter-residue contacts for each residue
defining a spherical protein volume centered in the C atom (or C for GLY) and with a radius to 6.5

7. The Predicator Back-propagation
one hidden layer
two output neurons
The number of hidden neuron – from 2 to 32
The input window – 1 to 15 residue long
A cross validation procedure

8. Neural Networks Input Coding

10. Frequency Distribution of the Relative Solvent Accessibility

11. Frequency Distribution of the Number of Contacts