Search and analysis of identical reverse octapeptides in unrelated proteins.

ABSTRACT: For the past few decades, intensive studies have been carried out in an attempt to understand how the amino acid sequences of proteins encode their three dimensional structures to perform their specific functions. In order to understand the sequence-structure relationship of proteins, several sub-sequence search studies in non-redundant sequence-structure databases have been undertaken which have given some fruitful clues. In our earlier work, we analyzed a set of 3124 non-redundant protein sequences from the Protein Data Bank (PDB) and retrieved 30 identical octapeptides having different secondary structures. These octapeptides were characterized by using different computational procedures. This prompted us to explore the presence of octapeptides with reverse sequences and to analyze whet

SUBMITTER: Saravanan KM 

PROVIDER: S-EPMC4357837 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature