Enzyme: Crystal Structure of Wild-Type Human Phosphoglucomutase-1 (PGM1) the description of the mechanism of how this enzyme is regulated (e.g., depending on the enzyme, the mechanism could range from being solely dependent on gene regulation to protein structure-based mechanism).
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Enzyme: Crystal Structure of Wild-Type Human Phosphoglucomutase-1 (PGM1)
the description of the mechanism of how this enzyme is regulated (e.g., depending on the enzyme, the mechanism could range from being solely dependent on gene regulation to protein structure-based mechanism).
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- CENTRAL DOGMA & STRUCTURE-FUNCTION RELATIONSHIPS IN PROTEINS You are a bacteriologist studying a pathogenic protein (the "BAD" protein) that contributes to diseases caused by Staphylococcus aureus. BAD functions as an aß heterodimer, and the a subunit (25kD) and ß subunit (75KD) are held together by an electrostatic interaction between K in the a subunit and D in the B subunit. You are trying to dissociate the BAD subunits to prevent pathogenesis in the bacteria. Which mutation would you make to prevent the BAD subunits from forming a dimer? Assume neutral pH. (A) introduce AAA → AGA point mutation in the a subunit gene (B) introduce GAC → GAG point mutation in the ß subunit gene (C) introduce GAT → CGT point mutation in the ß subunit gene (D) introduce two point mutations: AAG → GTG in the a subunit gene & GAC → CTC in the B subunit gene (E) introduce two point mutations: AAA → TGC in the a subunit gene & GAT → TGT in the B subunit gene second base in codon A TGT Cys TGC Cys TTT Phe…Protein folding with PDI and Peptidyl-prolyl isomeraseComponents of Complex Biomolecules Figure 1-10 (Lehninger's Biochemistry book) shows the major components of complex biomolecules. For each of the two important biomolecules below (shown in their ionized forms at physiological pH), identify the constituents. And show H-bonding with water. (a) Guanosine triphosphate (GTP), an energy-rich nucleotide that serves as a precursor to RNA: N- NH -CH2 0- NH2 H H H H. ОН ОН (b) Phosphatidylcholine, a component of many membranes: CH3 O- CH3*N-CH2-CH2-0-P-0–CH2 нн CH3 НС —О—С—(CH), —С—С— (CH), — СHз CH,–0-C-(CH,)14–CH3
- The allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!resting state of the protein, the Lys 216 Schiff base has pKa = 9.5 and Asp 85 has pKa = 3.5. When the conformational change occurs, the proton that was on the Schiff base moves to Asp 85. This should tell you that one or both of these two pKas changed with the conformational change. How does the pKa of Asp 85 compare with the pKa of the Lys 216 Schiff base after the conformational change?Purification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…
- Drawing the Structure of a Glycopeptide (Integrates with Chapters 4and 5.) Consider the peptide DGNILSR, where N has a covalentlylinked galactose and S has a covalently linked glucose. Draw thestructure of this glycopeptide, and also draw titration curves for theglycopeptide and for the free peptide that would result from hydrolysis of the two sugar residues.Protein,nfolded Proteinţolded Under certain conditions, a specific protein has the following thermodynamic parameters for going from the unfolded state to the folded state: AH = – 300 kJ/mol, and TAS = – 400 kJ/mol. Under those conditions, the equilibrium would lie more toward neither would predominate - the fraction of total protein that's folded would = fraction unfolded. the folded state the unfolded state O It is impossible to predict the position of the equilibrium from AH and TAS.Please select appropriate word in each bracket Many anti-cancer drugs affect nucleotide metabolism and inhibit DNA synthesis. For example, a widely used anti-cancer agent, 5-fluorouracil, is a pyrimidine analog that is incorporated into nucleotide form and affects DNA synthesis by inhibiting the activity of [ Select ] ["thymidine kinase", "ribunucleotide reductase"] , the enzyme required to synthesize [ Select ] ["dTMP", "dUMP"] . This inhibition of DNA replication affects both cancer and normal cells, and hence there are serious side effects of these agents including [ Select ] ["immune system suppression", "hyperallergenic reaction"] and damage to the [ Select ] ["lining of the GI tract", "connective tissue of cartilage"] . Methotrexate, was the first drug to actually cure a cancer, choriocarcinoma, in 1958, and serves to block the activity of [ Select ] ["dihydrofolate reductase", "serine hydroxymethyl-transferase"] , another enzyme required for the synthesis of dTMP.
- Peptide mass determination. You have isolated a proteinfrom the bacterium E. coli and seek to confirm its identityby trypsin digestion and mass spectrometry. Determinationof the masses of several peptide fragments has enabled youto deduce the identity of the protein. However, there is adiscrepancy with one of the peptide fragments, whichyou believe should have the sequence MLNSFK and an(M 1 H)1 value of 739.38. In your experiments, yourepeat edly obtain an (M 1 H)1 value of 767.38. What isthe cause of this discrepancy and what does it tell youabout the region of the protein from which this peptide isderived?Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?Part C Using the values of pKas in the table below, calculate the pI for DTLH. Properties of some amino acids found in proteins Name Aspartic acid Abbreviations: 1- and 3- letter codes D, Asp Histidine H, His Leucine L, Leu Threonine T, Thr ΓΙ ΑΣΦ Submit pKa of a-COOH pKa of a-NH3+ pKa of lonizing Group Group Side Chain Express your answer to two significant figures. Request Answer 2.1 1.8 2.4 2.6 ? 9.8 9.2 9.6 10.4 3.9 6.0
