Describe one advantage and one disadvantage of trying to solve molecular protein structures

Posted: September 22nd, 2022

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Step 1: All of the questions for the week are in a single Discussion post – you need to provide a short a succinct answer to each of my questions. Be brief and accurate using ~3-4 sentences for each answer, although longer is fine if needed. Number each of your answers to match my numbered questions; week 1 question 1 is 1.1, week 1 question 2 is 1.2, etc. You will not receive credit if you copy the answers directly from the textbook or from another student, including a shared internet resource – write the answers in your own words.
Step 2: Choose one of my questions to write a follow-up question to and include your question at the bottom of this same post “My follow-up question to RLM question 1.1 is:…”
Protein Purification Methods
Q4.1- What chemical properties of sodium dodecyl sulfate (SDS) contribute to equal charge/mass ratios needed for molecular mass determinations using SDS-PAGE? Why is the protein solution heat denatured prior to gel loading?
Peptides & X-ray/NMR Methods
Q4.2- Describe one advantage and one disadvantage of trying to solve molecular protein structures by 1) X-ray crystallography and by 2) Nuclear Magnetic Resonance (NMR) spectroscopy.
Functional Classes of Proteins
Q4.3- For each of the five major protein types in eukaryotic cells 1) provide a specific example of a protein in each class, 2) describe its primary function, and 3) identify cellular locations where you would find this specific protein (nucleus, cytosol, membranes).
Structure and Function of Hemoglobin
Q4.4- In addition to O2, another diatomic molecule that can bind to the iron atom in hemoglobin is CO. Explain in biochemical terms why high levels of CO gas are lethal and cite a specific example of accidental death by CO poisoning (where/when/how).

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