Is the histidine side-chain pKa value higher, lower, or unchanged in an environment surrounded by arginines? Explain your answer.
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- In TLC, why are the colors of the peaks for each amino acid are different depending on the types of amino acid?In BLOSUM62 matrix, a conserved Tryptophan position has score S(W,W) = 11, but a conserved Leucine position has score S(L,L) = 4. Give at least one reason why these values differ.If an extra nucleotide is inserted in the first exon of the beta globin gene, what effect will it have on the amino acid sequence of the globin polypeptides? Will the globin most likely be fully functional, partly functional, or nonfunctional? Why?
- A protein substrate is known to be multi-monoubiquitinated. The control lane "C" in the SDS-PAGE gel shows a properly ubiquitinated protein substrate. Please draw out what the lane would look like if all lysine residues except for one are mutated to alanine residues in the protein substrate. Use one sentence to explain your rationale. C 1 Protein Substrate ||||The proximal histidine residues have been replaced by glycine residues by mutation of the cloned genes for both the α and β subunits of hemoglobin. With the tetrameric mutant hemoglobin (all subunits being mutant, α H F8 G, β H F8 G), it was found that the “proximal” coordination bonds to hemes in the mutant protein could be replaced by having the small molecule imidazole in the buffers. Oxygen binding curves for the tetrameric mutant hemoglobin were measured. A. The degree of cooperativity in oxygen binding for the mutant hemoglobin (with imidazole present) would be expected to 1) increase 2) decrease 3) not be affected) compared with the normal protein. B. Justify your answer to part A in terms of what you know about the structural basis of cooperativity in hemoglobin. C. How would the Hill coefficient for the mutant be expected to change compared with nH for normal hemoglobin, which is ~3?What are the primary proteolytic enzymes used to degrade immunoglobulin molecules into definable fragments to facilitate the study of their structure? Beside each peptide bond-splitting enzyme, indicate the number of fragments they produce after digestion.
- In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%You have discovered a novel protein that has a pI = 5.5. To study the functional properties of this new protein, your research group has made a mutant that contains two amino acid changes—namely, a surface Phe residue in the normal protein has been replaced by His (side chain pKa = 6.1) and asurface Gln has been replaced by Glu (side chain pKa = 6.0). Is the pI of themutant protein predicted to be greater than, less than, or the same as the pIof the normal protein? Support your answer with the appropriate calculationThe a chain of eukaryotic hemoglobin is composed of 141 amino acids. What is the minimum number of nucleotides in an mRNA coding for this polypeptide chain?