<?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-tuzun-guvener</title><link>https://pages.htgaa.org/2026a/tuzun-guvener/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 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 (Ala to Val 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/tuzun-guvener/homework/week-05-hw-protein-design-part-ii/index.xml" rel="self" type="application/rss+xml"/></channel></rss>