<?xml version="1.0" encoding="utf-8" standalone="yes"?><rss version="2.0" xmlns:atom="http://www.w3.org/2005/Atom"><channel><title>Week 5 HW: Protein Design Part II :: 2026a-zarias-arman-aelius-saadatkhah</title><link>https://pages.htgaa.org/2026a/zarias-arman-aelius-saadatkhah/homework/week-05-hw-protein-design-part-ii/index.html</link><description>Part A: SOD1 Binder Peptide Design Superoxide dismutase 1 (SOD1) is a cytosolic homodimeric antioxidant enzyme that converts superoxide radicals (O₂⁻) into hydrogen peroxide and molecular oxygen. It coordinates copper and zinc ions essential for catalysis and structural integrity. The A4V mutation — Alanine → Valine at residue 4 of the mature protein (residue 5 in the UniProt P00441 precursor) — causes one of the most aggressive familial ALS subtypes by subtly destabilizing the N-terminal β-strand and promoting toxic SOD1 misfolding and aggregation.</description><generator>Hugo</generator><language>en</language><atom:link href="https://pages.htgaa.org/2026a/zarias-arman-aelius-saadatkhah/homework/week-05-hw-protein-design-part-ii/index.xml" rel="self" type="application/rss+xml"/></channel></rss>