<?xml version="1.0" encoding="utf-8" standalone="yes"?><rss version="2.0" xmlns:atom="http://www.w3.org/2005/Atom"><channel><title>SOD1 Binder Peptide Design :: 2026a-flo-razoux</title><link>https://pages.htgaa.org/2026a/flo-razoux/homework/week_05_hw/sod1-binder-peptide-design/index.html</link><description>Intro from Pranam Chatterjee Superoxide dismutase 1 (SOD1) is a cytosolic antioxidant enzyme that converts superoxide radicals into hydrogen peroxide and oxygen. In its native state, it forms a stable homodimer and binds copper and zinc. Mutations in SOD1 cause familial Amyotrophic Lateral Sclerosis (ALS). Among them, the A4V mutation (Alanine → Valine at residue 4) leads to one of the most aggressive forms of the disease. The mutation subtly destabilizes the N-terminus, perturbs folding energetics, and promotes toxic aggregation.</description><generator>Hugo</generator><language>en</language><atom:link href="https://pages.htgaa.org/2026a/flo-razoux/homework/week_05_hw/sod1-binder-peptide-design/index.xml" rel="self" type="application/rss+xml"/></channel></rss>