Can someone help me please **Bio 206 Lab Exam 1**Instructions: Answer these questions in a detailed but concise manner on a separate paper. You may include labeled drawings or tables, if helpful. **Short answers, not long essays.**1. **Is the way a protein folds random? What factors or forces determine it?**2. **Explain what is meant by an enzyme’s optimal temperature and explain what happens if the enzyme solution is too cold or too hot. Define what is meant by an enzyme’s optimal pH and explain why extreme pH’s denature most enzymes.**3. **Explain the roles of the following components of the bacterial transformation / pGLO experiment: ampicillin, LB broth, heat shock, arabinose, UV light.**4. **We use methylene blue and Janus B Green to stain plant cells and animal (our cheek) cells. What did each stain and which one changed color? What did the color change indicate?**5. **Consider the action potential simulation (neuron). The rising portion of the graph of an action potential represents the depolarization of the neuron. Which channels are active during this portion of the graph, and what happens to the charge of the neuron at that location? The falling portion of the graph represents the repolarization of the neuron. Which channels are active during this portion of the graph, and what happens to the charge of the neuron at that location?**6. **We modeled Cystic Fibrosis in lab. What is the main problem with someone with Cystic Fibrosis? What ion is involved and what happens as a result of this ion? Be specific.**7. **What determines the resolution limit of a microscope? Is the purpose of the fluorescence microscope to increase the magnification beyond that of a typical light microscope? Why or why not?**8. **Explain the mechanisms of the four types of fluorescence microscopy we discussed in lab: 1) GFP fusion proteins 2) immunofluorescence – direct and indirect, 3) mitotracker, and 4) phalloidin.**9. **Explain the mechanisms of the three types of ELISA we discussed in lab: 1) direct, 2) indirect, 3) sandwich. Which type of ELISA did we do in lab? What is one advantage of this kind of ELISA?**10. **What are negative and positive controls, and why are they

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Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Countless trillions of chemical reactions take place daily in our bodies to support vital metabolic functions. Enzymes are proteins that interact with substrate molecules to stabilize the transition state and lower the activation energy required for a chemical reaction to occur. Through stability, reaction rates accelerate and reach physiologically important rates. At critical places in their structures known as active sites, enzymes bind substrates. They frequently have a very narrow range of substrates to which they will attach. Most metabolic processes would take much longer to complete without enzymes and would be too slow to support life.

Oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases are the six major types of enzymes. Within its own category, each category performs a single broad type of reaction while catalyzing numerous more specialized reactions. Apoenzymes are enzymes that are inactive until they are bound to a cofactor, at which point they become active. Metal ions (such as Zn) or organic substances that bind to the enzyme covalently or noncovalently can both serve as cofactors. A holoenzyme is the name given to the cofactor and apoenzyme combination.

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