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Protein Charge Interaction Analysis of SEP, TPO, and PTR Residues: Phosphorylated and Non-Phosphorylated Sites

Analyze charge interactions in proteins containing SEP, TPO, and PTR residues using PISCES server. Compare phosphorylated and non-phosphorylated sites. Calculate charges for each phospho-site.

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Protein Charge Interaction Analysis of SEP, TPO, and PTR Residues: Phosphorylated and Non-Phosphorylated Sites

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  1. RCSB proteins containing SEP, TPO, PTR residues PISCES server 90%, 25% id: Min L 40 aas: Res limit 3.0 A Phosphorylated Non-Phosphorylated SEP TPO PTR SEP TPO PTR 100% 86 90 112 4381 3918 2972 90% 40 25 47 1757 1425 996 25% 29 14 13 912 800 500 Calculate charge interactions with protein for each real and control phospho-site (2- at site)

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