3 and 4 Aging related proteins of vertebrates like Silurana tropi

3 and 4 Aging related proteins of vertebrates like Silurana tropicalis 5 have also been sequenced, but without structures. S. tropicalis is an amphibian, mostly found in tropical and subtropical regions, is a significant model for genetics due to its close evolutionary AG14699 relationships with humans and experimentally tractable nature. It is the only Xenopus species having diploid genome and whose whole genome has been sequenced. Moreover, this genus is commonly used in the investigations of human disease genes such as nephronophthisis, studying the connection between these disorders,

ciliogenesis and Wnt signaling etc. Thus an attempt has been made to predict structures of aging related proteins of S. tropicalis using different selleck chemicals bioinformatics tools and to validate their efficiency. The complete protein sequences of aging related proteins of S. tropicalis were downloaded from Uniprot. 6, 7 and 8 Total 5 protein sequences were found and downloaded by protein knowledgebase (UniProtKB) pipeline; prohibitin 2 (301 aa) [UniProt: A9UMS3 PHB2_XENTR], serum response factor-binding protein 1 (535 aa) [UniProt: Q5XGC9 SRFB1_XENTR], reactive oxygen species modulator 1 (79 aa) [UniProt: A4QNF3 ROMO1_XENTR], CDGSH iron–sulfur

domain-containing protein 2 [Uniprot: Q51027 CISD2_XENTR] and an uncharacterized protein (668 aa) [F6YQA9 F6YQA9-XENTR]. The UniProt is a collective database of protein sequence and protein annotation data. Protein structure homology modeling of the proteins was done using “automated mode” in SWISS-MODEL.9, 10 and 11 As a rule of thumb, for a sufficiently reliable alignment of automated sequences the identical residues of target and template must share more than 50%.12 The automated template selection has approved the template structures only with high-resolution with reasonable stereo chemical properties which were assessed by ANOLEA,13 QMEAN14 and Gromos96.15 The protein homology structures

were evaluated using two online software; ERRAT and RAMPAGE. ERRAT16 is a protein structure verification algorithm. ERRAT runs by statistical analysis of non-bonded interactions Dipeptidyl peptidase between different types of atom. It generates a single output plot showing the error value to the residue window. By statistical data comparison with highly evaluated structures, it generates the error values to yield the confidence limits. This is extremely beneficial to test the homology model reliability (ERRAT v2.0). RAMPAGE17 is an online server which designs a Ramachandran plot from the input data by plotting phi (φ) versus psi (ψ) dihedral angles of each residue. The plot is divided into three distinct regions: allowed, disallowed and favored regions based on density dependent plotting of the residues.

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