Structure prediction and refinement of protein sequence to identify intrinsically disordered regions of islet amyloid polypeptide (IAPP) using in-silico approach.

IAPP, or Islet Amyloid Polypeptide, is a protein that plays a crucial role in type II diabetes. The purpose of this work is to investigate IAPP from a structural and sequential perspective. Various Research Methods and Instruments including: In this instance, we acquired a sequence from UniProt and then used Alphafold to create a prediction about the structure of the sequence. Therefore, the execution of the FG-MD algorithm is not possible because there are no disorder regions present. Based on the findings, it can be concluded that the PROTPARAM server was utilised for the purpose of sequential analysis. Our submission of the genomic sequence of the IAPP protein was made through the usage of this site. We utilised the Phyre2 server in order to carry out the structural analysis. This prediction offers the pdb file for the protein that is anticipated to be the target. An examination of the structure was carried out with the help of a Ramachandran plot validation, which made use of saves. Ramachandran plot analysis was the method that we utilised in order to complete our investigation into the structure of the IAPP protein. Because of this, a structure that is both compact and extremely precise is required in order to validate the target protein (IAPP). [ABSTRACT FROM AUTHOR]