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- 2. The diagram to the right shows the change in the structure of the C-terminal portion of each of the ẞ-subu- nits of human hemoglobin (HbA) in the oxyHb to deox- yHb or R-to-T transition. The hydrogen bonding interac- tion of the C-terminal ẞHis 146 residue with the side chain of Asp94, highlighted by the red ellipse, has been shown to be responsible for a major portion of the proton uptake associated with the Bohr effect. Treatment of HbA with the enzyme carboxypeptidase A (CPA) results in loss of the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ- subunits. (a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y = fraction of heme groups occupied by O2] to compare the values of the Hill coefficient nн and the O2-binding affinity at pH 7.4 of normal HbA before and after treat- ment of with CPA. (b) (' ) How will the plot for CPA-digested HbA change at pH 7.2? (c) 1 Hi5146 HN- ✓ Low PK B-chain. CH2 CH-NH-CO-CH-NH- CH₂ Tyr145 он HbO2 or R state Туг145 CH-CH2- OH co NH CH CH₂ His…3. The trp repressor is a homodimer with 107 amino acid residues per monomer. The content of proton dissociable groups of each monomer is given below: Side chain pKa number/monomer ZpH 4 ZpH 6 12.5 Arginine Aspartate Glutamate 9. 4.0 4.0 10 Histidine 6.0 2 Lysine Tyrosine -NH3® 10.0 6 9.5 2 7.0 1 -СООН 4.0 1 (a) ( : ) The isoelectric point (pl) of the protein, i.e., the pH at which the overall electrostatic charge on the protein E z = 0, is 5.3. Although the pKa values in the table above are only approximate values generally characteristic of residues with unhindered exposure to solvent, confirm that the overall charge on the protein must pass through zero between pH 4 and pH 6. ) Estimate what must be the average pKa value of all of the residues containing carboxylic (b) ( acid groups using the H-H equation below, assuming that the pka values of the positively charged groups do not change from the values given in the table above: pH pKa log [base]/[acid] + DNA te5-Bromouracil is an analogue of thymine that usually pairswith adenine. However, 5-bromouracil frequently pairs withguanine. Explain.
- 3. Draw both hemiacetal forms of d-ribofuranose and both hemiacetal forms of d-xylofuranose.The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. ()9. The T conformation of the hemoglobin tetramer is stabilized (in part) by a salt linkage between the side chain of the lysine residue at position 40 in the a-chain of one aß dimer and the C-terminal carboxylate group of the ß-chain of the opposing aß dimer. Draw a diagram of this salt linkage (show complete side chains).
- Draw the structure of a phosphonamidite monomer suitable for SPPS of adenosine RNA Nucleosides. Circle all protecting groups and identify their canonical deprotection conditions.In Figure 1-8b, can you tell if the number of hydrogenbonds between adenine and thymine is the same as thatbetween cytosine and guanine? Do you think that aDNA molecule with a high content of A + T would bemore stable than one with high content of G + C?What are the term of anticodon loop?
- 1. A certain polypeptide was treated with trypsin and yielded the following Fragments: Leu-Glu Gly-Tyr-Asn-Arg Gln-Ala-Phe-Val-Lys The same polypeptide was treated with chymotrypsin and yielded the following fragments: Gln-Ala-Phe Asn-Arg-Leu-Glu Val-Lys-Gly-Tyr What is the amino acid sequence of this polypeptide? Instructions Make use of the table below to determine the sequence of the mystery protein.2. Draw the structure of pentapeptide Trp-Asp-Cys-Lys-Gln that would predominate in aqueous solution at pH=5.5. (Relevant pKa values are 2.2, 3.8, 8.3, 9.6 and 10.5.)8.Iron-uptake protein IupA is a human 302-aa, N-glycosylated, heterodimeric protein of considerable therapeutic interest. It contains 3 disulfide bridges that stabilise its structure. Explain what expression host you would use to produce the protein in recombinant form.