complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.

Q: Under certain conditions, peptide bond formation rather than peptide bond hydrolysis is…

A: Peptide bond formation- A peptide bond is a chemical bond formed between two molecules when the…

Q: amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the…

A: Phenyl isothiocynate is the Edman reagent. It reacts with N-terminal amino acid to give phenyl…

Q: running the reaction at 83 °C cooling the reaction to 11 °C changing the pH to 5.4 Increase reaction…

A: The rate of an enzyme catalyzed reaction depends on various factors like temperature and pH of the…

Q: Chymotrypsin is a pH dependent protein. Enzymatic activity is the greatest between pH=7.0 to pH=8.5.…

A: Chymotrypsin is a protease that is secreted by the pancreas. It cleaves the peptide bond next to the…

Q: if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine…

A: Serine protease are the enzymes that cleave peptide bonds in proteins in which serine serves as…

Q: You have obtained a 10X fold purification and a yield of 10% at the Affinity step. What was the…

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Q: There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for…

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Q: The following data describe the catalysis of cleavage of peptide bonds in small peptides by the…

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Q: The rate of the peptidyl transferase reaction increases as the pH increasesfrom 6 to 8. Explain…

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A: The reaction mechanism which follows general acid-base catalysis is as follows.:

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Q: Amino acids can be prepared from a-halo carboxylic acids [RCH(X)COOH] by reaction with excess NH3.…

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Q: Consider the ff dissacharides. a. Classify the glycosidic linkage as α or β and use numbers to…

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Q: 3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however…

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Q: Polyvinyl acetate

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Q: Saccharide X occurs in the roots of several species of plants. Deduce the structure of saccharide x…

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Q: Identify on the structure below, the amide bond which will break during the inhibition of…

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Q: A biochemist is trying to determine the type of proteases they have isolated from walrus blubber.…

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Q: A synthetic substrate, the para-nitrophenylacetate (PNPA), is used to monitor enzyme activity of…

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Q: Draw structural formulas for the products obtained when the tripeptide Thr-Leu-Ile undergoes…

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Q: Define aminoacyl (A) site

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Q: Draw the Haworth projection of β-D-Altopyranose given the structure of D-Altrose.

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Q: (EPR) which of Lactobacillus casei fermentation of milk was found to have potent blood pressure…

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Q: 5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for…

A: Lineweaver-Burk Plot: This plot is also called as double reciprocal plot as equation for the plot is…

Q: Linear homoglycan of glucose connected by α1-4 linkages…

A: Polyssacharides are the long chains of carbohydrate molecules which are composed of several units of…

Q: Draw the structure of alpha-ketoglutarate that is generated in a reaction catalyzed by glutamate…

A: Glutamate dehydrogenase (GDH) catalyzes the conversion of glutamate into α-ketoglutarate. The enzyme…

Q: Identify the structure of O-a-D-sorbopyranosyl-(2 → 4)-B-D-glucopyranose below. The following…

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Q: dentify and describe how you would PEGylate this peptide at its N- terminal amine. Discuss the…

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Q: Write the structure formula, three-letter and one-letter abbreviation for each essential amino acid…

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