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- What is meant by the term "sugar code"? What are the challenges in the field of glyco-biology?Draw the Fischer Projection, Haworth and Chair conformation for D-GlucosePolypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.
- Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa value of the side chain, suggest a reason why is this so?Draw the Haworth projection of the following sugar molecules: D-galactose D-fructose D-mannoseChart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?
- Would you expect lysozyme to hydrolyze cellulose? Why or why not?Diagram the cyclization of monosaccharides which leads to the formationof pyran rings. Required: Please show me a correct and step by step process of the diagram and show me the correct drawing of the pyran ring.The oxyanion hole of a serine protease has which of the following roles (select all correct answers)? Question 3 options: Acid-base catalysis Proximity and orientation effects Transition state stabilization Induced fit
- a protease that cleave peptide bonds adjacent to aspartate and glutamate would likely have an s1 pocket that contain positively charged amino acids true or false3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however they are a structurally diverse family of enzymes especially in the organization of the active site amino acids. A group of scientists have reported a potential drug molecule based on a binding study using circular dichroism. They report that the molecule binds to the active site. Can the experiment support the claims, why or why not? Which techniques might be used to support this claim?Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.