<?xml version="1.0" encoding="utf-8" standalone="yes"?><rss version="2.0" xmlns:atom="http://www.w3.org/2005/Atom"><channel><title>Lab (Week 10) — Mass Spectrometry :: 2026a-sergio-cuiza</title><link>https://pages.htgaa.org/2026a/sergio-cuiza/labs/lab-week-10--mass-spectrometry/index.html</link><description>Completion status:
This lab was completed theoretically (no physical or virtual wet lab performed). All procedures, data, and analyses below are based on the provided protocol, the figures in the Appendix, and standard LC-MS principles. The report follows the logical progression from intact mass determination to native/denatured comparison, peptide mapping, and CDMS analysis of megadalton complexes. Introduction and Background Modern bioengineering relies on precise protein characterization. Liquid chromatography–mass spectrometry (LC-MS) provides three critical pieces of information: molecular weight, amino acid sequence, and protein folding/structure. This lab introduces LC-MS using enhanced Green Fluorescent Protein (eGFP) and Keyhole Limpet Hemocyanin (KLH). The workflow proceeds from intact protein analysis (denaturing and native conditions) to bottom‑up peptide mapping, and finally to charge detection mass spectrometry (CDMS) for megadalton complexes.</description><generator>Hugo</generator><language>en</language><atom:link href="https://pages.htgaa.org/2026a/sergio-cuiza/labs/lab-week-10--mass-spectrometry/index.xml" rel="self" type="application/rss+xml"/></channel></rss>