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Does the selected Job Description meet all, most or some (or a %) of the basic requirements found in the text? Is it presented in a way that you find it a benefit for recruitment or not?

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Job Description Analysis

Compare the characteristics of Practice Manager – Primary & Specialty Care (provided below), content, specificity or generality with the sample job description below.

Beyond the comparison, be sure to answer the following:

  • Does the selected Job Description meet all, most or some (or a %) of the basic requirements found in the text?
  • Is it presented in a way that you find it a benefit for recruitment or not?
  • Are there key features it adds that actually enhance the text sample?

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

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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.

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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?

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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.

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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.

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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.

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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.

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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?

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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.

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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?