Concept explainers
To write:
Post translational modification via Michael addition.
Introduction:
The tricarboxylic acid (TCA) cycle consist of a series of various
The Krebs cycle is called as the citric acid cycle as the
The Michael reaction also known as Michael addition in which there is addition of a nucleophile of a carbanion takes place to the a, ß unsaturated carbonyl compound.
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Biochemistry
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- A family of proteins known as cupredoxins contain a single redoxactive Cu ion coordinated by a Cys, a Met, and two His residues. The reduction potentials of cupredoxins range from about 0.15 V to 0.68 V. What does this information reveal about the role of the protein component of the cupredoxins?arrow_forwardWhy is the position of Cys 58 important in 3GRS(GLUTATHIONE REDUCTASE)? When Cys 58 is mutated to GLY 58 how would it impact the 3D structure and function of 3GRS? explain in terms of how Cys and GLY have different properties and how it would impact the function of 3GRS (the binding sites etc.) You can see your structure(3GRS ) here or any other website: https://www.rcsb.orgarrow_forwardcis-Vaccenate is an 18-carbon unsaturated fatty acid abundant in E. coli membrane lipids. Propose a metabolic route for synthesis of this fatty acid, in light of the fact that stearic acid, the C18 saturated analogous fatty acid, is virtually absent from E. coli lipids.arrow_forward
- A binding curve for the binding of the amino acid tryptophan to the protein called TxtE is shown below. Estimate the association equilibrium constant (Ka; in units of M-1) for Trp binding to TxtE.arrow_forwardBovine pancreatic trypsin inhibitor (BPTI; as shown) contains six cysteine residues that form three disulfide bonds in the native structure of BPTI. Suppose BPTI is reduced and unfolded in urea (as illustrated for RNase A as shown). If the reduced unfolded protein were oxidized prior to the removal of the urea, what fraction of the resulting mixture would you expect to possess native disulfide bonds?arrow_forwardShown to the right is a cartoon image of ETC Complex I from Y. lipolytica. A group of authors studied this wild type Complex I and also a version where the arginine at position 121 in the chain 3 subunit was mutated to a methionine (R121M). Part of chain 3 subunit contains the peptide sequence SMITH a. Draw the titration curve for the SMITH peptide. Mark all pKa’s and the pI on your curve. For the SMITH peptide at physiological pH, explain what types of interactions you believe the side chains are or are not able to participate in.arrow_forward
- The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.arrow_forwardProtein hydrolysis is an exergonic process,yet the 26S proteasome is dependent on ATP hydrolysis for activity. (a) Explain why ATP hydrolysis is required by the 26S proteasome. (b) Small peptides can be hydrolyzed without the expenditure of ATP. How does this information concur with your answer to part a ?arrow_forwardGlobular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning