Ethics emphasizes happiness, justice, human rights, and equality. How do these ideas relate to the environment and future generations? Support your perspective using ethical theorie(s).

Discuss the pros and cons of the federal, state, and local government funding human service programs. Should they continue to do so, or should it be the responsibility of concerned citizens to “care for their own”?

You are the Executive Director of Human Resources for the College of New Caledonia. There is a global pandemic called COVID-19 causing unprecedented disruption to society, business operations, and global economies. Everyone is feeling the impact and no one is immune to this including your organization CNC. The President of the College of New Caledonia has asked you as the Executive Director of Human Resources to prepare a Human Resources Pandemic Plan for the organizations COVID-19 response. To create a comprehensive plan, you are required to pay particular attention to a few key details that will impact employees.

In your plan, briefly discuss the following topics (and provide your reasoning):

1. Compensation plans for employees - is peoples pay changing as a result of disrupted work? (Strategic Pay Plans)
2. Employee benefits and services plans for employees - is this changing as a result of disrupted work? (Employee Benefits and Services)
3. Health and Safety decisions made to protect employees. (Occupational Health & Safety Chapter 10)
4. Union partners collaboration and communication – what is the plan for how you work with the unions? (Labour relations)
5. What will happen if employees are non-compliant with recommendations or are not able to work to expected standards? (Performance Management)

4. The S1 pocket of serine proteases

a. is where the proper substrate binds

b. is the catalytic triad

c. determines which amino acid side chain is bound

d. all of the are true

e. none of the above are true

5. With respect to aspartyl proteases

a. the use a zinc to make alkoxide

b. they use an activated hydroxyl made from water

c. they form a transient covalent bond with the peptide being cut

d. all the above are true

e. none of the above are true

6. With respect to restriction enzymes

a. their action is inhibited by methylases

b. only animals use them as a defense system

c. they act by cutting RNA at specific nucleotide sequences

d. all of the above are true

e. none of the above are true

A.  Suppose that the sequence below was the open reading frame of a gene. It’s not the entire mRNA molecule, just the protein coding sequence and in this case the first three bases is the start codon. The sequence is given as DNA sense strand because DNA is where mutations happen.  

5’-ATGTCTAAACTGCGTGAGTAA-3’

i.  Give the sequence of the polypeptide it encodes. Make sure to mark the carboxyl and amino terminal ends.

ii.   Give a mutant version of the second codon that has a single base substitution that is a synonymous mutation.

iii.   Give a mutant version of the fourth codon that has a single base substitution that is a missense mutation.

iv. Write a mutant version of the entire sequence that is an example of an in frame insertion. Indicate what part of the sequence is different.

(1) _____How are proteins normally resident in the ER retrieved when they escape the ER? (please explain why)

A. They have short amino acid sequences that serve as retrieval sequences.

B. Specific receptors bind to soluble proteins to return them to the ER in COP-I vesicles.

C. Specific receptors bind to soluble proteins to return them to the ER in COP-II vesicles.

D. Both A and B are correct.

(2) What is the major difference between glycosylation of proteins in the ER and glycosylation of proteins in the Golgi complex?

(3) Some proteins are imported into their appropriate organelle after they are created in the cytosol. This is done by different mechanisms for the different organelles. Compare and contrast the mechanisms, noting which ones have similarities and which ones have differences.

1. When mRNAa are being translated simultaneously by multiple ribisomes, the structure is known as a(n)__.

a- operon

b - polytene

c- polycistron

d- polyribosome

e- copolymer

2. which of the following is not involved in the initiation of translation in bacteria?

a- mRNA

b- tRNA carrying N-formylmethionine that will occupy the P site

c- GTP and initiation factors

d- small and large ribosomal subunits

e- tRNA carrying the next amino acid that will occupy the A site

3- what type of proteins recognize and bind to eukaryotic upstream regulatory promoter consequences sequences

a- sigma subunits

b- RNA polymerase III

C- All of these proteins can bond to the regulatory promotor sequences

d- Rut proteins

e- transcriptional proteins

The chemical 5-amino-2,3-dihydro-1,4-phthalazinedione, better known as luminol, is used by forensic scientists in analyzing crime scenes for the presence of washed-away blood. Luminol is so sensitive that it can detect blood that has been diluted 10,000 times. A basic solution of luminol is often sprayed onto surfaces that are suspected of containing minute amounts of blood. Luminol has a molecular weight of 177 g/mol.Before investigating the scene, the technician must dilute the luminol solution to a concentration of 2.00×10−2 M . The diluted solution is then placed in a spray bottle for application on the desired surfaces. How many moles of luminol are present in 2.00 L of the diluted spray? Express your answer with the appropriate units.

Trypsin and chymotrypsin are members of the family of serine proteases. They cleave peptide bonds at the C-terminal end of specific residues. Chymotrypsin recognizes aromatic residues, while trypsin recognizes lysine and arginine. The recognition of a particular side chain (side chain specificity) is fully determined by the structure and properties of the binding pocket. In the case of chymotyipsin the binding pocket is hydrophobic and is wide enough to accommodate an aromatic ring. Given what you know about the properties of Lys/Arg side chains, what can you say about the size/shape and possible interactions that would provide the substrate specificity in the case of trypsin? What amino acid residues from the trypsin molecule would you expect to find in the binding site?