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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…2. The mature form of TEM-1 ß-lactamase, an enzyme of 290 amino acid residues that hydrolyzes penicillin antibiotics. The protein has the following polar amino acid side chains: 18 Arg; 11 Lys; 6 His; 4 Tyr; 16 Asp; 20 Glu; 8 Asn; 5 Gln. Approximate pKa values 1.5 Arginine 12.5 Lysine 10.0 Histidine 6.5 OD 280nm Tyrosine 10.0 Aspartate or Glutamate 4.0 Terminal NH3+ 8.0 Terminal COOH 4.0 0.0 A 0.01 0.10 KCI B Volume (mL) The chromatogram above shows a typical result in the purification of TEM-1 ß-lactamase overex- pressed in E. coli cells. The protein is eluted from an anion exchange column at pH 6.25 with an increasing gradient of KCI. Fraction A is shown to correspond to native enzyme. Since Fraction B has the same amino acid sequence for the first 10 residues, the conclusion is that this fraction represents enzyme in which side chains of glutamine or asparagine residues have been hydrolyzed (deamidated). (a) ( ) What is the isoelectric point of the native enzyme? (b) ( ) Compared to…2. The mature form of TEM-1 ß-lactamase, an enzyme of 290 amino acid residues that hydrolyzes penicillin antibiotics. The protein has the following polar amino acid side chains: 18 Arg; 11 Lys; 6 His; 4 Tyr; 16 Asp; 20 Glu; 8 Asn; 5 Gln. Approximate pKa values 1.5 Arginine 12.5 Lysine 10.0 Histidine 6.5 OD 280nm Tyrosine 10.0 Aspartate or Glutamate 4.0 Terminal NH3+ 8.0 Terminal COOH 4.0 0.0 Α - 0.01 0.10 KCI B Volume (mL) The chromatogram above shows a typical result in the purification of TEM-1 ß-lactamase overex- pressed in E. coli cells. The protein is eluted from an anion exchange column at pH 6.25 with an increasing gradient of KCI. Fraction A is shown to correspond to native enzyme. Since Fraction B has the same amino acid sequence for the first 10 residues, the conclusion is that this fraction represents enzyme in which side chains of glutamine or asparagine residues have been hydrolyzed (deamidated). (a)( ) What is the isoelectric point of the native enzyme? (b)( ) Compared to…
- Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (c) Outline how you would investigate whether BCMAP would be an effective inhibitor for the protein in competition with the molecules that the protein normally targets, and any solvent. Figure 1. 4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and brown, respectively) in the active site of the protein structure.Please give me all answer 1 . Which one of the given amino acids has a sulfur atom?A. cysteineB. serineC. glutamineD, leucineE. proline 2. The hydrogen bonding between the carbonyl group of an amino acid with the amino group of the fourth amino acid farther along the chain leads to __A. parallel ẞ-pleated sheetsB. antiparallel ẞ-pleated sheetsC.a-helixD.B -helixE. none of these 3. Which of the choices is a class of complex lipids?A. steroidsB.terpenesC. waxesD.prostaglandinsE. furansexpanded structure of the D-tagatose Fischer projection of D-tagatose Haworth projection of D-tagatose
- 1. H3N a. Draw the peptide sequence, including stereochemistry (wedges and dashes) for Glu-Cys- Gly. The N-terminus is drawn for you as a starting point.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).2. As we've seen previously, peptide bonds involving the amino acid proline can populate both "trans" and "cis" isomers. trans-Pro cis-Pro This isomerization reaction can be the rate-limiting step in protein folding. Depending on the protein sequence, the relative favorability of the trans and cis states can change. For Pro-117 in the protein staphylococcal nuclease, the rates of the forward and reverse reactions are: ktrans→cis = 3.1 × 10-2 and kcis→trans = 2.5 x 10-3 s-1. (a) What is AG°' for this reaction? (b) A prolyl isomeriase enzyme increases the rate of the forward reaction to kcat.trans->cis = 2.6 s-1. What is the new rate constant for the reverse reaction (kcat,cis→trans)? (c) This prolyl isomerase is a Michaelis-Menten enzyme with kcat = 2.6 s!, KM = 1.9 µuM. If you have 1 nM enzyme, what is Vo for [S]o = 0.7 µM? What about [S]o = 30 µM? For each condition, what limits the reaction speed?
- 2. Amino acid analysis of the a heptapeptide gave the following residues: Asp Glu Leu Lys Met Tyr Trp NH4+. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was OH H C-C-CH₂ H. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Glu, Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a tetrapeptide that had a net positive charge at pH 7 and tripeptide that had a zero net charge at pH 7. What is the amino acid sequence for this heptapeptide?Modify methionine to show its zwitterion form. Select Draw с N 0 Templates S H More 1C || H0 C 1 с | CH₂ | CH₂ | S 1 CH3 HIN I N-H Erase Q 2 Q15. Which of the following glycans can be released from proteins using BB- elimination? a. Complex N-linked glycans b. Glycosaminoglycans c. Mucin type O- glycans d Hyaluronic acid 16. Which of the following glycans are made by the addition of sugars to the reducing end of a growing glycan chain? a. Hyaluronan b. Heparan sulfate c. Mucin type O-glycans d. Gangliosides e. Cellulose 17 Name the following ganglioside using GNX nomenclature? 200