Related Experiment Video
Updated: Jun 25, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
A simple derivation of the distribution of pairwise local protein sequence alignment scores
1CNRS (UMR 5168) - INRA (UMR 1200) - CEA - Université Joseph Fourier, Laboratoire de Physiologie Cellulaire Végétale; CEA Grenoble, 17 rue des Martyrs, F-38054, Grenoble cedex 09, France. olivier.bastien@cea.fr
Abstract:
Confidence in pairwise alignments of biological sequences, obtained by various methods such as Blast or Smith-Waterman, is critical for automatic analyses of genomic data. In the asymptotic limit of long sequences, the Karlin-Altschul model computes a P-value assuming that the number of high scoring matching regions above a threshold is Poisson distributed. Using a simple approach combined with recent results in reliability theory, we demonstrate here that the Karlin-Altshul model can be derived with no reference to the extreme events theory.Sequences were considered as systems in which components are amino acids and having a high redundancy of Information reflected by their alignment scores. Evolution of the information shared between aligned components determined the Shared Amount of Information (SA.I.) between sequences, i.e. the score. The Gumbel distribution parameters of aligned sequences scores find here some theoretical rationale. The first is the Hazard Rate of the distribution of scores between residues and the second is the probability that two aligned residues do not lose bits of information (i.e. conserve an initial pairing score) when a mutation occurs.
More Related Videos
16:02Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
Published on: February 10, 2023
05:08Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
Published on: July 8, 2025
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Distribution of Molecular Speeds
Conservation of Protein Domains
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Extraction: Partition and Distribution Coefficients
For extracting a solute from an aqueous phase into an organic...
Protein Organization
The primary structure of a protein is its amino acid sequence.
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...