This is BIOchemistry) For the appetite-related signaling molecule MELANOCORTIN:

a.) What is the specific function of that molecule?

b.) What is the mechanism of that action (how does it do what it does)?

c.) How is that molecule made? Describe any prepro- and pro- forms and associated cleavages or covalent bonds or phosphorylations associated with the molecule.

d.) Describe how the molecule is regulated

(This problem relates to chapters 22, Biosynthesis of amino acids, nucleotides, and related molecules; and chapter 23, hormonal regulation and integration of mammalian metabolism, from the Lehninger Biochemistry textbook).

You perform a cell free translation experiment like Nirenberg and Matthaei, but you forget to write down what nucleotides you added to make the mRNA. You precipitate the translated polypeptides and measure the relative amount of radiolabeled amino acids incorporated into them. You get 25% proline, 25% threonine, 12.5% glutamine, 12.5% lysine, 12.5% asparagine, and 12.5% histidine. What nucleotides and in what % did you add to make the mRNA? Please explain step by step.

Why is the answer 50% C and 50% A?

Which statement is TRUE regarding the late stages of starvation?

A) The brain has decreased its need for glucose by switching to lactate as a major energy source.

B) HIgh levels of acetyl-CoA derived from lipid catabolism lead to the production of acetoacetate.

C) Ketone bodies are produced from amino acids liberated from noncritical proteins.

D) Gluconeogenesis is extremely active in the liver because of the large amounts of lactate exported from the muscle.

E) Catabolism of triacylglycerols provides the major source of a gluconeogenic metabolite in the form of glycerol.

For each item, select "Absorptive" or "Post-absorptive" depending on which state is correct.

What are the differences between polyamides and proteins ? I) Polyamides are unable to undergo hydrogen bonding between individual polymer chains. II) Polyamides usually do not have hydroxyl- or thiol-groups as side chains. III) Proteins and polyamides can be partially crystalline. IV) Polyamides have a more stable bond between their monomers than proteins have between the individual amino acids.

Choose one answer.

A. I and II
B. II and III are correct
C. II and IV
D. III and IV

You have an opportunity to invest $51000 now in return for $601000 in one year. If your cost of capital is 7.6%​, what is the NPV of this​ investment?

Calculate the double integral ∫∫Rxcos(x+y)dA∫∫Rxcos⁡(x+y)dA where RR is the region: 0≤x≤π3,0≤y≤π2

If from 2g of sucrose (M = 342 Da) 0.8ml of ethanol was obtained (density = 0.8 g / ml; M = 46.07 Da), what is the Yield of the process?

1. What type of reaction links two amino acids into a dipeptide?

2. What functional groups are found in the peptide backbone?

3. Would a peptide in solution be vulnerable to cleavage by addition of a strong base to the solution?

4. Where does the R group or side chain connect to the backbone of an amino acid?

5. Are polypeptides linear or branched polymers?

6. Where are hydrophobic side chains generally found in a globular protein?

7. Where are hydrophilic side chains generally found in a globular protein?

8. What non-covalent interaction stabilizes an alpha helix?

9. What non-covalent interaction stabilizes an beta sheet?

10. What is the most important feature of primary structure?

11. What mediates the formation of tertiary structure in a polypeptide or protein?

12. What distinguishes quaternary structure from tertiary structure?

13. What non-covalent interactions are disrupted when a protein is denatured?

14. What amino acid residues participate to form a disulfide bond?

15. Does a protein that exists as a monomer have quaternary structure? Explain your answer, a simple yes or no will receive no credit?