ABSTRACT

Bioinformatics is the application of statistics and computer science to the field of molecular biology. The Challenge of Bio-Informatics is the rationalization of mass of sequence Information, with a view not only to deriving efficient means of data storage but also to design analysis tools. The Smith-Waterman algorithm is a well-known algorithm for performing local sequence alignment. that is, for determining similar regions between two nucleotide or protein sequences. Instead of looking at the total sequence, the Smith-Waterman algorithm compares segments of all possible lengths and optimizes the similarity measure. Homology modeling, also known as comparative modeling of protein refers to constructing an atomic-resolution model of the "target" protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein (the "template"). Homology modeling relies on the identification of one or more known protein structures likely to resemble the structure of the query sequence, and on the production of an alignment that maps residues in the query sequence to residues in the template sequence. It has been shown that protein structures are more conserved than protein sequences amongst homologues, but sequences falling below a 20% sequence identity can have very different structure, and reach what is called in homology modeling, the twilight zone

(Guide Signature)

(Coordinator Signature)

ABSTRACT
Bioinformatics is the application of statistics and computer science to the field of molecular biology. The Challenge of Bio-Informatics is the rationalization of mass of sequence Information, with a view not only to deriving efficient means of data storage but also to design analysis tools. The NeedlemanWunsch algorithm performs a global alignment on two sequences (called A and B here). It is commonly used in bioinformatics to align protein or nucleotide sequences. The algorithm was published in 1970 by Saul B. Needleman and Christian D. Wunsch[1]. Homology modeling, also known as comparative modeling of protein refers to constructing an atomic-resolution model of the "target" protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein (the "template"). Homology modeling relies on the identification of one or more known protein structures likely to resemble the structure of the query sequence, and on the production of an alignment that maps residues in the query sequence to residues in the template sequence. It has been shown that protein structures are more conserved than protein sequences amongst homologues, but sequences falling below a 20% sequence identity can have very different structure, and reach what is called in homology modeling, the twilight zone

(Guide Signature)

(Coordinator Signature)