Posts

Write a 5 paragraph essay (600 word minimum) stating the main role as well as overlapping duties of the following health professions.

/in /by

Comparative Research

Write a 5 paragraph essay (600 word minimum) stating the main role as well as overlapping duties of the following health professions.

1- Physician Assistant VS. Nurse (DNP/FNP or ARNP) (First paragraph)

2- EMT (or EMS) VS. Firefighter (First responder) (second paragraph)

3- Physical Therapist VS. Occupational Therapist (Third Paragraph)

Conclude with your personal opinion or inclination to any of these professions and why. If neither of these professions are of your interest then tell me which is and why. (Citation is needed and copy/paste will be penalized as it will be scanned for plagiarism). Assignments will not be accepted after the due date.

Develop at least three possible discussion questions that you can discuss to help everyone understand the main points of the assigned reading.

/in /by

Discussion leader

Develop at least three possible discussion questions that you can discuss to help everyone understand the main points of the assigned reading. Don’t worry about the small details. Your task is to help people mull over the big ideas in the reading and to share reactions to the text. Prepare your own brief answers to your questions. You be responsible for creating thought provoking questions to help your teammates analyze the reading. You will need to turn in at least three discussion questions with your own brief answers.

What are the strongest reasons for why companies whether founder / family-owned or public – should adopt corporate governance best practices?

/in /by

ACC 530: Company Founder Outlines Reservations about Corporate Governance

  • https://www.studypool.com/questions/download?id=2757733&path=uploads/questions/5818700/20230227194839mini_case_study_1_organica.pdf&fileDownloadName=attachment_1

Questions to Focus Discussion
What are the strongest reasons for why companies whether founder / family-owned or public – should adopt corporate governance best practices?
What critical challenges emerge in promoting good corporate governance in your region?
What are the obstacles? How difficult are those to address and overcome?
How would you implement reforms to achieve adherence to good corporate governance

Using the information provided, create accurate staffing, performance and operating budgets.

/in /by

Finance Question

Requirements: In order to successfully complete this project, you must meet the following criteria. Using the information provided, create accurate staffing, performance and operating budgets. You are required to use Microsoft Excel to complete the final product. You are required to use the most effective formulas in the spreadsheet program. Spreadsheets without correct and appropriate formulas are literally worthless and can cause financial losses for organizations. Therefore, spreadsheets without appropriate and correct formulas will receive a score of zero (0). The budgets should be formatted professionally. The spreadsheet should include columns and amounts for weekly and annual totals only for both individual employees (on the staffing budget) and grand totals, where appropriate.

Briefly explain the origins of CRT, what CRT is, what proponents of the theory aim to achieve, and why this area of study is considered so controversial. Conclude with your own thoughts on this subject.

/in /by

Critical Race Theory

  • Write two full pages, no more and no less.
  • Use double spacing and 12-point Times New Roman font.
  • Format your document with 1” margins on all sides.
  • Include in-text citations.
  • Use two to four scholarly sources (journal articles, academic books).
  • Place your references on a separate Works Cited page.
  • Follow the MLA 8 style guide.
  • 0 pt spacing between paragraphs

In recent years, critical race theory (CRT) is being taught in more schools across the West. However, CRT remains a highly contentious topic. Briefly explain the origins of CRT, what CRT is, what proponents of the theory aim to achieve, and why this area of study is considered so controversial. Conclude with your own thoughts on this subject.

Provide Evidence. Analyze the Evidence (be sure to cite) and explain how it supports the main idea of the paragraph.

/in /by

Article Writing Question

Along with your page numbers, make sure you have all of the following:

  • Your Name
  • My Name
  • Class
  • Date

Centered Title: The Wonderful World of Essay Two Reminders.

Remember to use standard paragraphing meaning you start with an indented paragraph. Be sure you have completed all the unit assignments including Discussion Board participation and dropbox assignments. That will help get the essay where it needs to be! Remember, you are writing a review on a segment of Last Week Tonight with John Oliver. You are not writing an essay on the topic he addresses. The essay should be 3-4 pages.

1. Have a hook that draws in your audience

2. Start general and get more specific and lead into an introduction of John Oliver and Last Week Tonight. Who is he, what is his purpose. Undoubtedly you will have to address his humor.

3. You need 2 sources with in-text citation that will look something like this (Faries). One source should address Last Week Tonight with John Oliver directly, and the other should address his topic. You will use both sources to support any claims you make about the nature of the segment and its subject matter.

4. Close with a powerful thesis that sets up your body paragraphs. YOU MAY WANT TO CONSIDER A TWO PARAGRAPH INTRO.

5. Do you have a clear topic sentence for every paragraph that makes a claim and is tied to your thesis?

6. Introduce your support (evaluate the evidence using the CRAP method) and be compelling about it (Use the MEAL Plan).

7. Provide Evidence.

8. Analyze the Evidence (be sure to cite) and explain how it supports the main idea of the paragraph.

9. Conclude and link back to thesis and next paragraph.

10. Repeat this in at least 3 body paragraphs.

11. You must have support in EVERY paragraph. It can be the same source, but just remember you need at least two additional sources beyond the John Oliver segment we are exploring. One should address him or the show, and the other should address his topic.

12. The first paragraph will be a general conclusion of the segment and its purpose, while the final paragraph will be a broader conclusion on the topic and a possible call to action. You should incorporate your outside sources into one of these paragraphs as well.

Work Cited

Oliver, John. Host. “Policing.” Last Week Tonight. Season 4, Episode 114. HBO. Oct. 8, 2017.

Youtube. https://www.youtube.com/watch?v=J5b_-TZwQ0I

Write an essay explaining what is science in your simple words.

/in /by

What is science

Write an essay explaining what is science in your simple words.

How many monomers (also called subunits) are in this protein? Are they similar in shape or dissimilar? How many individual polypeptide chains are in this protein?

/in /by

Protein Folding

Part I:  Protein Folding

The shiga-like toxin (ST) is a protein-based toxin produced by the bacterium Enterohemorrhagic Escherichia coli (EHEC), which is the causative agent responsible for most cases of bloody diarrhea.  Believe it or not, much of the disease symptoms associated with EHEC infection derives from the cytotoxic effects of ST, whose protein ribbon structure is shown below.  Analyze these images (both the side and bottom view) and answer the following questions:

Side View                                                                           Bottom View

 

  1. (2 points) How many monomers (also called subunits) are in this protein?  Are they similar in shape or dissimilar?
  2. (2 points) How many individual polypeptide chains are in this protein?
  3. (2 points) How many unique polypeptide chains do you think are in this protein?
  4. (2 points) What type of structure is shown here (1o, 2o, 3o or 4o)?
  5. (2 points) What would be a good descriptive (but scientific) classification for this protein?  Hint:  Consider our description of hemoglobin as it pertains to the nature and number of subunits contained therein.
  6. (3 points) Identify two different forms of secondary structure in this protein (use arrows and label them appropriately).  If one type of secondary structure is not present, indicate so in your answer below.

Part II:  Enzymatic Active Site Motifs

Below is an image of an enzymatic active site, which is occupied by the enzyme’s substrate (shown below, left).  This enzyme catalyzes the reaction that changes cyclic AMP (shown in the active site) to AMP.

 

Cyclic CMP

 

  1. (3 points) Explain why this enzyme cannot bind to cyclic CMP and catalyze the reaction that would change cyclic CMP (shown above, right) to CMP.  Please be specific in your answer.
  2. (3 points) What would happen to the enzyme’s affinity for cyclic AMP if the enzyme’s active site had a missense mutation that changed the Threonine residue (blue) to Valine?  Briefly explain your answer.
  3. (3 points) What would happen to the enzyme’s affinity for cyclic AMP if the enzyme’s active site had a missense mutation that changed the Serine residues (orange and dark green) to Threonine?  Briefly explain your answer.
  4. (3 points) Take a closer look at the active site for this enzyme and examine the noncovalent interaction mediated by the residue highlighted in pink.  Is it possible for a mutation to alter this residue in such a way as to eliminate this noncovalent interaction with cyclic AMP?  Briefly explain your answer.

 

Part III:  Multimerization

Protein families arise when a protein sequence that generates a stable fold diverges over many generations and acquires new functions.  One example of this can be seen in the globin family.  Myoglobin (shown below, left) is a stable monomeric protein that can help carry oxygen using a heme molecule (cofactor).  On the other hand, hemoglobin (shown below, right) is only functional as a tetramer and while it also uses heme to carry oxygen, it is useful over a much more dynamic range than myoglobin.  The “globin fold” is structurally conserved across these proteins, but the ability to tetramerize arose through genetic drift and natural selection.

  1. (5 points) Thinking back about what we learned about DNA sequence mutations and their effect on protein structure, provide an explanation for how changes in the polypeptide sequence of these two proteins can still produce the same overall fold (i.e. alterations that conserve protein structure) but have slight differences in the protein’s ability to multimerize (i.e. alterations that alter protein-protein interactions).
  • Another way to think about this is to consider what kind of mutations might promote multimerization (polar vs. nonpolar) in an aqueous environment and where would you expect these changes to be within the overall protein structure (surface vs. core)?

 

 

BONUS (1 point):  Considering their structure (and what you know about synthesizing polypeptide chains), hypothesize why proline residues are often positioned at sharp turns in the polypeptide sequence.  Why might that be the case?  Hint:  try drawing a tripeptide chain where proline is the second residue.

 

Briefly summarize the data shown in the figure. Be sure to compare the phenotypes from the bacterial strains where the GOI was deleted vs. the bacterial strains where individual amino acid substitutions were introduced into the GOI.

/in /by

Biochemical Pathways

Below are representative transmission electron micrographs (TEM) of the WT and mutant P. gingivalis strains as well as quantitative data that measures the quantity of OMVs produced by these bacterial strains.  To generate the graph, please note that the Alaei lab used a fluorescent probe to quantitate the relative levels of OMVs produced by the WT or mutant P. gingivalis strains.  Use this data to answer the following questions.

 

1. (2 points) Briefly summarize the data shown in the figure.  Be sure to compare the phenotypes from the bacterial strains where the GOI was deleted vs. the bacterial strains where individual amino acid substitutions were introduced into the GOI.

 

2. (2 points) Provide a hypothesis that could have been tested using this experiment.  Your hypothesis should include a potential function for the protein encoded by the GOI.  In other words, how might this gene be involved in OMV production?

 

3. Let’s consider the possibility that GOI encodes a phosphatase. Recall that phosphatases are enzymes that dephosphorylate proteins or other biomolecules.  For the sake of simplicity, assume that this phosphatase catalyzed half of the reaction shown below (i.e. the enzyme removed one of the phosphate groups on the molecule shown on the left):  2H2O ++ 2HPO42-

  • (3 points) Given that the GOI product is a phosphatase, would you assume that the reaction shown above is exergonic or endergonic?  Explain your reasoning.
  • (3 points) Porphyromonas gingivalis lives exclusively in mammalian hosts.  Would you expect the phosphatase encoded by GOI to be active at -20oC?  How about 150oC?  Explain your reasoning.
  • (3 points) Given their phenotypes, did the single amino acid substitutions (R88A, H116A and H157A) alter the catalytic activity of this phosphatase?  What level(s) of protein structure (primary, secondary, tertiary, quaternary) would you expect to be altered by mutations that impact phosphatase activity?  Briefly explain your answer.
  • (3 points) Based on what you know about enzymes (and the phenotypes associated with the mutant gingivalis strains), where in the protein might the amino acid substitutions be located?  Why would altering protein structure at this site result in the phenotypes that you see illustrated in the figure?

Hint: what is a common structural feature of enzymes that facilitates their role in catalyzing chemical reactions?

 

4. (4 points) Do the single amino acid substitution (R88A, H116A and H157A) mutants display the same phenotype as the null mutant strain (i.e. the mutant strain where the GOI was deleted)?  What about genotypes (are they the same or different)?  Briefly explain your answer.

 

5. (4 points) If Dr. Alaei’s research group had already discovered that deleting the GOI caused the phenotype shown above, why would they want to study the single amino acid substitution mutants?  What would this add to our understanding of the mechanism driving OMV formation.

 

6. (4 points) Consider the specific amino acids that were mutated in the gingivalis mutants (R8A, H116A and H157A).  Describe the nature of the mutations (how do the R-groups of substituted amino acids differ from the amino acids that they replaced) and predict whether these specific mutations are likely to have impacted the primary, secondary, tertiary and/or quaternary structure of the phosphatase encoded by the GOI.  Explain your reasoning.

 

7. (2 points) What type of point mutations do you think underlie the amino acid substitutions in the GOI (conservative/nonconservative missense, nonsense, silent, frameshift)?  Explain your reasoning.

 

BONUS (1 point):  The substrate of the phosphatase encoded by the GOI is not a protein (see Q#3).  What larger macromolecule or cell structure might that molecule be a part of and how could modulating its phosphorylation level modulate budding of vesicles off the bacterial cell surface?

 

The Krebs cycle adds a 2-carbon molecule to a 4-carbon molecule to produce a 6-carbon molecule. If we wanted to create an alternative cycle that uses 10-carbon input molecules, what could the rest of the Krebs cycle intermediates be?

/in /by

Lab 7:  Understanding Cellular Respiration

 LAB GOALS:

  • To understand the logic of the process of cellular respiration.
  • To conquer the fear and loathing of navigating these biochemical processes & pathways!

 OUTLINE:

  1. Overview and Introduction
  2. Glycolysis
  3. Krebs Cycle
  4. Electron Transport and Oxidative Phosphorylation
  5. Putting it all together!

INTRODUCTION:

Today we are going to use simple problem-solving techniques to figure out how our cells can dismantle the glucose molecule to provide energy in the form of ATP.  Although it can look daunting at first, these processes actually follow a logical progression that can be deciphered without too much agony.

STOW AWAY ALL YOUR NOTES & DEVICES!  USE LOGIC ONLY FOR THIS ACTIVITY!

 

PART 1:  Glycolysis

Obtain a GLYCOLYSIS packet for your group.  This packet should contain:

  • 9 Green Cards
  • 4 Yellow ATP Cards
  • 1 Yellow NAD Card

(It’s a good idea to check before you start that you have all the necessary cards.)

On the mitochondrion mat, order the green cards to show the 9 steps of glycolysis.  This is a problem-solving exercise, not a memorization test.  You should be able to order the green cards without any prior knowledge of glycolysis solely by elimination and chemistry logic.  The final solution will make sense with the arrows on the laminated map.  You can start adding the yellow cards where they make sense.

NOTE:  Biological chemistry is driven by carbon and phosphate.  If you try to keep track of hydrogen or oxygen, these reactions will drive you crazy!  Why?  Because we are working in an aqueous environment and parts of water molecules are enveloping all the reactants almost all of the time.  Focus on carbon!

When you arrive at a Glycolysis pathway that you think is correct, ask your instructor to check your progress.  If you have not yet arrived at the correct pathway order, keep working until you do!  When you arrive at a correct pathway, do a ‘speed round’ by mixing up the cards and trying to recreate the correct solution as quickly as possible.  Less than 20 seconds is good.  (The reason we do this is not to encourage speed-memorization, but to practice logic at high speeds, which is a different method for challenging our brain to make sense of a complicated pathway).

When you have finished, discuss the following questions briefly with your group.  Answers are located on the last page of this guide.

 

Glycolysis Discussion Questions:

  1. In step 3, there is an arrow between reactant and product. Does this arrow signify an enzyme?
  2. There are two ATP-spending cards in this process, and two ATP-creating cards. Is this process ‘ATP neutral’?
  3. [A really hard thought question] Which of the enzymes in Glycolysis do you think evolved earliest?

 

After you have finished with the Glycolysis packet, replace all of the cards in the packet and exchange it for a Linking Step & Krebs Cycle Packet.

 

 

PART 2:  Arranging the Krebs Cycle and Linking Step

Check to make sure your Linking Step & Krebs Cycle Packet contains:

  • 12 Red cards of varying sizes
  • 6 Yellow cards (1 ATP, 4 NADH and 1 FADH2)

Now that you’ve practiced some problem-solving with the Glycolysis Packet, you are ready for an even more difficult challenge.  Starting with pyruvate (which you might recognize as the 3-carbon molecule that was the end result of glycolysis) you should attempt to place the cards in order through the Linking Step and the Krebs Cycle.

You’ll need to create a Krebs Cycle that can be repeatedly loaded with input molecules.  Notice that there is a circular pathway that is ‘fed’ by the linking step.  The molecules you chose to be the reactants in the step that starts this circular pathway need to correspond to the larger molecule that starts the cycle.  In other words, what you put in should correctly start the series of reactions.  When you find the correct solution, this will make sense.

At some points in this cycle, redox reactions will take place.  Occasionally, we need to determine whether a redox reaction has occurred between organic molecules that have the same number of carbons.  We have a specific algorithm for this:

  1. Count the C-H bonds in the reactant.
  2. Count the C-C bonds in the reactant.  Double bonds count as 2 C-C bonds.
  3. Add these numbers together to get the ‘Reactant High Energy Bond Number.’
  4. Count the C-H bonds in the product.
  5. Count the C-C bonds in the product.  Double bonds count as 2 C-C bonds.
  6. Add these numbers together to get the ‘Product High Energy Bond Number.’
  7. If the Reactant High Energy Bond Number does not equal the Product High Energy Bond Number, then a redox reaction has occurred.

Does this algorithm make sense to you?  This is a formal way of deciding whether the energy state of a molecule has changed simply by counting the bonds that tend to have more energy in them (C-C and C-H).  You may need this algorithm to determine where to place certain yellow cards in this packet.

NOTE:  The electron-carriers FADH2 and NADH can be tricky.  Each carries a hydrogen and 2 electrons.  Each is reduced to their energy-carrying form by oxidizing carbon.  The energy levels of these two carriers are slightly different (as we will see in the Electron Transport Chain).  However, there is no logical reason that you should be able to determine which redox step is FADH2 rather than NADH.  Your instructor will help you with this detail.  This is due simply to a difference in the enzyme used to catalyze that step.

Use of the lower-output FADH2 may be a way to protect against poisons or mutations that might damage NADH usage (an internal redundant system).  It may also be vestigial; we may simply be in the process of evolving towards use only of higher-energy NADH and this is the last enzyme that has yet to make the evolutionary switchover.  Like many evolutionary questions, we don’t know for sure (and the scope of this question is a bit beyond this class).

CoA-containing intermediates have a high-energy S-C bond.  In one place, this high-energy bond is used to create an important C-C bond.  In another place, CoA-C energy is released in a catalyzed reaction that produces GTP.  GTP is of similar energy to ATP, and is converted quickly to that more common energy currency.

When you arrive at a Krebs Cycle that you think is correct, ask your instructor to check your progress.  If you have not yet arrived at the correct pathway order, keep working until you do!  When you arrive at a correct pathway, do a ‘speed round’ with the Krebs Cycle.  Less than 25 seconds is good.

When you have finished, discuss the following questions briefly with your group.  Answers are located on the last page of this guide.

 

Linking Step and Krebs Cycle Discussion Questions:

  1. Give a one-sentence basic summary of the purpose of the Krebs Cycle.
  2. The Krebs cycle adds a 2-carbon molecule to a 4-carbon molecule to produce a 6-carbon molecule. If we wanted to create an alternative cycle that uses 10-carbon input molecules, what could the rest of the Krebs cycle intermediates be?  (There are many possible answers.)
  3. What is the major difference in the linking step between prokaryotes and eukaryotes? In which type of cell is the linking step probably more difficult to carry out?

After you have finished with the Linking Step & Krebs Cycle Packet, replace all the cards and exchange it for an Electron Transport & Oxidative Phosphorylation Packet.

 

 

PART 3:  Re-Enacting the Electron Transport Chain

Make sure your Electron Transport & Oxidative Phosphorylation Packet contains:

  • 8 Blue or Purple cards of varying sizes
  • 3 Yellow Cards
  • A handful of small H+ and e- cards

You’ve already recreated the processes that have led to the production of reducing equivalents in the form of NADH and FADH2.  In this third packet, you’ll demonstrate the use of those electrons to produce a proton gradient which will be used to create ATP.

Begin by placing the complexes in the mitochondrial membrane of your laminated eukaryotic cell.  NADH drops off two electrons and a proton at Complex I, while FADH2 electrons and protons are added to Complex II.  Both Complex I and II can then transfer electrons to a slightly lower energy state on Coenzyme Q.  Electrons move from higher energy states to lower energy states from this mobile protein Q to Complex III to mobile protein Cytochrome C to Complex IV.  At Complex IV, electrons are transferred to the extremely low energy electron acceptor O2.

During this process, the energy of the electrons is used to transport protons to the inner mitochondrial membrane at Complexes I, III and IV.

NOTE:  In prokaryotes, this process occurs in the cellular membrane.  While essentially the same, the key difference is that prokaryotes are pumping protons into the outer environment, ending up with a net gradient inside the cell that is relatively low in protons, pulling protons back into the cell through ATP Synthase.

Demonstrate the flows of electrons, protons and the changing ATP/ADP molecules as the process continues first for NADH, and then repeat the demonstration for FADH2.  You should be able to watch the membrane gradient build up and then recover.  All group members should feel comfortable leading this demonstration and talking through the process.  When you feel comfortable with your understanding of this process, demonstrate it for your instructor with input from all group members.  When your instructor is confident in your understanding, move on to the following discussion questions.

Electron Transport & Oxidative Phosphorylation Discussion Questions:

  1. Why are electrons delivered via NADH more valuable than those delivered to the ETC via FADH2?
  2. What is the role of oxygen in cellular respiration?
  3. How are the ETC complexes arranged in the inner mitochondrial membrane?

After you have finished with the Electron Transport & Oxidative Phosphorylation Packet, replace all the cards and put it back in the piles with the other packets.