The Relationship Between The Amino Acid Residues Of Context And The Secondary Structure Of Protein Of Target Sequence

According to the extraction of sequence fragments together with thecontinuity of secondary structure of protein and the diversity of secondarystructure was analyzed the relationship between the polarity of amino acidresidues of context and the secondary structure of protein of target sequence in967non-redundant protein sequences using computer software. To determinehow the secondary structure of protein will be affected by the amino acidresidues of context of the target sequence. And then the target sequences wereclassified in accordance with the polarity classification, and further analyzed.After classification of the target sequence, the effect of the probability ofperformance is more obvious.All data used in this article are from the PDB (Protein Secondary StructureDatabase) database, where SCOP database was selected as the secondarystructure classification database, and secondary structure definition database wasselected as the DSSP (protein secondary structure definition database) database.The dates from internet were converted, into the original database. According tothe original database and the homology of the original database, the database of967non-redundant data was obtained in this article. In order to reduce theredundant data of the original database error in the final analysis of data.The analysis software used in this paper was developed in the underDelphi7development platform, a small data processing software.In the analysis process, we found the formation of secondary structure of aprotein sequence fragments, was not only rely on their own factors, but also relyon its neighboring amino acid residues. Making the secondary structure of thetarget sequence fragments tend to the secondary structure of continuity under theinfluence, may also make the secondary structure of the target sequencefragments tend to be continuous secondary structure. But, its structure must showa certain degree of diversity. We found that the relationship between theprobability of this effect and the polarity of amino acid residues, when the polarity of the adjacent amino acid changed, the secondary structure of the targetsequence fragment there was a high probability of change. Specific secondarystructure and the corresponding probability will be described below.The focus of this paper was to provide help for the prediction of proteinsecondary structure, the innovation lies in the formed external causes of thesecondary structure of the protein sequence fragments as the starting point forresearch. The conclusion will contribute to the prediction of protein secondarystructure as a reference data.