<?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-nathaniel-nainggolan</title><link>https://pages.htgaa.org/2026a/nathaniel-nainggolan/homework/week-05-hw-protein-design-part-ii/index.html</link><description>Part A.	SOD1 Binder Peptide Design (From Pranam)
Part 1: Generate Binders with PepMLM
This homework starts by opening the protein database UniProt to copy the FASTA format of the AA sequence of Superoxide dismutase (SOD1). According to UniProt, Superoxide dismutase functions as a catalyst for the oxidation of hydrogen sulfide (H2S) to sulfate, playing a crucial role in detoxifying H2S and limiting the accumulation of reactive sulfur species (RSS). It is an enzyme critical for destroying free radicals produced within cells, which are toxic to biological systems. As such, mutations to the gene that encodes the enzyme come with their own potential health complications. One such mutation is the alanine to valine mutation at codon 4 (A4V) of SOD1. It is a mutation that causes a rapidly progressive dominant form of amyotrophic lateral sclerosis (ALS). ALS is a terminal disease that causes the progressive loss of motor neurons, which leads to paralysis and death (Saeed et al., 2009). The images below show the AA sequence of the normal SOD1 protein along with its mutated counterpart.</description><generator>Hugo</generator><language>en</language><atom:link href="https://pages.htgaa.org/2026a/nathaniel-nainggolan/homework/week-05-hw-protein-design-part-ii/index.xml" rel="self" type="application/rss+xml"/></channel></rss>