19. For Huntington’s disease, expansion of trinucleotide repeat occurs within the ORF causing the HTT protein to have many repeats of the amino acid glutamine, which in turn, causes the mutant protein to be toxic to neurons. Fragile X syndrome is also a trinucleotide repeat disease. How is the FMR1gene (or its gene product) affected in the case of fragile X syndrome?

20. Classify the mutation that causes sickle cell anemia three different ways.

21. Describe a cellular process that can lead to the conversion of a cytosine in a CpG sequence in the DNA to thymine.

19. For Huntington’s disease, expansion of trinucleotide repeat occurs within the ORF causing the HTT protein to have many repeats of the amino acid glutamine, which in turn, causes the mutant protein to be toxic to neurons. Fragile X syndrome is also a trinucleotide repeat disease. How is the FMR1gene (or its gene product) affected in the case of fragile X syndrome?

20. Classify the mutation that causes sickle cell anemia three different ways.

21. Describe a cellular process that can lead to the conversion of a cytosine in a CpG sequence in the DNA to thymine.

1). Where do the hydrophobic amino acid residues usually end up in a folded protein and why? How does hydrogen bonding play a role in stabilizing the beta-sheet structure? Where do the R groups then end up in this structural pattern?

2). Why is the alpha-helix so commonly found? Describe the structural basis of this conformation.

3). How do amyloid-beta peptides aggregate and eventually cause Alzheimer's disease? Where do the amyloid-beta peptides come form (what protein are they from and where is that protein normally found)?

Aminoheptanoic acid is step polymerized to a polyamide and the reaction has a second order dependence on the amino acid concentration. The following rate constants are known: k= 1.0x10-3 kg/(mol min) at 150 °C and k= 2.74x10-2 kg/(mol min) at 180 °C.

a) Write the balanced reaction equation for formation of the polyamide with molar mass of 12 737 g/mol.

b) Calculate the activation energy E and the collision frequency factor A for the reaction.

c) What conversion is needed to produce polymer with number average molar mass of 4240 g/mol?

You have recently identified a maternal effect mutation in Xenopus that results in a complete lack of endoderm. You map the mutation and find two genes with point mutations that change the amino acid sequence in the protein, but don’t know which mutation is causing the phenotype. Both genes have unknown functions. Design an experiment or series of experiments that would allow you to 1) discern which gene is the cause of the mutation, 2) determine if it most likely functioned as a cell autonomous determinant or morphogen, and 3) if this gene was sufficient promote endodermal fates

Explain the difference between each of the following:

GMO corn vs. golden bantam heirloom corn (in production for over 80 years) –

predation vs. parasitism

desert vs. grassland

2-Pick two (2) biomes AND explain the characteristics of each.

3-Using this codon chart, what m-RNA and amino acid chain would be produced from this DNA sequence?

TAC CAC CGG GTA   AAA

please answer all is due in a hour typing  

1. Draw a 4 AA residue generic polypeptide with R groups (R, no specific AA required) - label clearly.

a. the peptide bond

b. one pair of H bond donor and H bond acceptor

c. outline one amide plane

d. label phi and psi for one junction

e. using your drawing, explain why peptide bonds are nearly always trans

g. label the amino terminus and carboxy terminus

2. What information does the Ramachandran plot provide and what are its implications for protein folding?

Given the following sequence: LHYEAIAKAWNDAF

a. Classify each amino acid into polar, non-polar, & charged (at pH 7.0)–put a letter above each to show if polar (p), non-polar (n), or charged (c).

b.What are the ionizable groups?

c.What is the order of the pKaʼs going from low to high pH

d.What is the isoelectric point (pl) of this peptide?

e.At the pHʼs of 3, 6, & 9, what is the charge state?

f.What type of secondary structure would this peptide take and why?

g.How long would it be?

h.How many hydrogen bonds, at maximum

In regards to protein function:

A) For specific DNA binding proteins,

1. what is the structure of a typically DNA binding protein and how does it interact with DNA?

2. why is there a difference between the major and amino groove in terms of protein binding?

B) describe how the Lac repressor interacts with DNA to find its binding site

C) describe how a catalyst lowers the activation energy of a reaction

D) how is the structure of enzymes used to design drugs for diseases like HIV?

E) what are the three steps of motor protein action?