<?xml version="1.0" encoding="utf-8" standalone="yes"?><rss version="2.0" xmlns:atom="http://www.w3.org/2005/Atom"><channel><title>Camila Naranjo — HTBAA Fall 2026 :: camila-naranjo</title><link>https://pages.htgaa.org/2026b/camila-naranjo/index.html</link><description>About me I’m a biotechnology engineer from Ecuador, currently working as a lab assistant responsible for the molecular biology laboratory at Universidad Politécnica Salesiana (UPS). During my internships and undergraduate thesis, I worked on protein expression and purification in E. coli, which sparked my interest in molecular and synthetic biology more broadly. I’m especially drawn to biomanufacturing of recombinant therapeutics — figuring out how to make the molecules people need more accessible and scalable.</description><generator>Hugo</generator><language>en</language><atom:link href="https://pages.htgaa.org/2026b/camila-naranjo/index.xml" rel="self" type="application/rss+xml"/><item><title>Week 1 HW: Final Project Ideas</title><link>https://pages.htgaa.org/2026b/camila-naranjo/week-01-hw-project-ideas/index.html</link><pubDate>Mon, 01 Jan 0001 00:00:00 +0000</pubDate><guid>https://pages.htgaa.org/2026b/camila-naranjo/week-01-hw-project-ideas/index.html</guid><description>HTBAA Homework #1 Name: Camila Naranjo&#10;I would like to biomanufacture alpha-1 antitrypsin (AAT), a glycoprotein that protects the lungs from damage caused by proteolytic enzymes. The production of this glycoprotein is intended to improve the quality of life for people with alpha-1 antitrypsin deficiency, an inherited condition (1). Currently, the primary treatment for this disease involves repeated administration of donated AAT, so the biomanufacturing of alpha-1 antitrypsin could make treatment more available.</description></item><item><title>Week 2 HW: DNA Design</title><link>https://pages.htgaa.org/2026b/camila-naranjo/week-02-hw-dna-design/index.html</link><pubDate>Mon, 01 Jan 0001 00:00:00 +0000</pubDate><guid>https://pages.htgaa.org/2026b/camila-naranjo/week-02-hw-dna-design/index.html</guid><description>Part 1: Define your expression target What molecule are you expressing? I’m expressing alpha-1-antitrypsin, a glycoprotein encoded by the SERPINA1 mRNA (GenBank accession K01396.1; NCBI Gene ID 526). I used the mRNA-derived CDS rather than the genomic SERPINA1 sequence because it is already spliced, contains no introns, and can be cloned directly as a continuous open reading frame into an expression vector. This protein requires post-translational modifications, so I chose CHO cells as the chassis. Moreover, this host is easier to scale up than HEK 293 cells. The protein has to be secreted, and the sequence already includes the native signal peptide, which directs the protein to the secretory pathway and is cleaved to release the mature protein, so no additional signal peptide is needed. The sequence is the following:</description></item><item><title>Week 3 HW: Cell-Free Protocols</title><link>https://pages.htgaa.org/2026b/camila-naranjo/week-03-hw-cell-free/index.html</link><pubDate>Mon, 01 Jan 0001 00:00:00 +0000</pubDate><guid>https://pages.htgaa.org/2026b/camila-naranjo/week-03-hw-cell-free/index.html</guid><description>CFPS REACTION DESIGN FOR SFGFP, PETASE, RETEPLASE A. COMPARE CELL-FREE REACTION COMPOSITIONS 1. Why does the concentration of potassium glutamate and magnesium glutamate differ between compositions? Which is more sensitive? Potassium glutamate and magnesium glutamate contribute K⁺ and Mg²⁺ ions, respectively, which provide the ionic strength and the cofactors essential for activating the transcription and translation machinery, whilst the Glu⁻ anion is the predominant natural physiological anion in the cytoplasm of E. coli (1).</description></item><item><title>Final Project</title><link>https://pages.htgaa.org/2026b/camila-naranjo/final-project/index.html</link><pubDate>Mon, 01 Jan 0001 00:00:00 +0000</pubDate><guid>https://pages.htgaa.org/2026b/camila-naranjo/final-project/index.html</guid><description/></item></channel></rss>