State if/how Remedios' mutation changes the amino acid sequence and describe the effect that change has, if any, on the protein

4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…

b. Explain how Nirenberg and Leder/Matthaei were able to create many of the codon/amino acids found in the Genetic Code (i.e. what was their experimental set- up, how did they know if the codons matched, what were the knowns, and finally what codons did they struggle with and why).

4A. Write out the chemical equations (structures are not necessary) for the two steps in the reaction catalyzed by aminoacyl tRNA transferase. Include all products and reactants. Step 1: amino acid activation Step 2: aminoacyl transfer to the tRNA 4B. Write the chemical equation for the net reaction catalyzed by aminoacyl transferase. This can be determined by taking the sum of the two reactions above.

9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. ligand a. Briefly explain, in terms of Ka, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2

C. Two mutations are known in the population, one shaded in yellow and one in blue, shown on the TEMPLATE DNA sequence below. Ursula has a mutation in the yellow- shaded underlined nucleotide: instead of an A in this position, she has a T. 5' AATCATAACTCATTG 3' What type of mutation does Ursula have? Second position First position (5 000 0 UUU UUC phe UUA UUG COU leu CỰU CUC CUA COO CUG ADO AUU AUC ile nov AUA AUG met GUU GUC GUA GUG val UCU UCC UCA ser UCA UCG COU CCU cce CCC CCA pro CCA CCG ACU www ACC ACA ACG GCU GCC GCA GCG thr ala UAU tyr UAC UAA Stop UAG Stop CAU CAC his CAC CAA gin CAG AAU AAC asn AAC AAA lys AAG GAU GAC asp glu GAA GAG UGU UGC cys UGA Stop UGG trp CGU Missense Silent Nonsense Frameshift CGC CGA arg CGA CGG AGU AGC AGA AGG GGU GGC GGA GGG Initiation Termination ser arg gly DUAG DUMU DUAU DUAG Third position (3-end)

Hi, can you please explain the clinical significance of G protein mutations.

Discuss the difference between frameshift vs. substitution mutation and give an example of how frameshift can completely damage a protein while substitution could have no effect on the protein made.