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Why is a strong reducing agent, such as NaBH4, not suitable for use in the conjugation of an oligosaccharide to a protein?
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- What is Folate Trap ? Explain the importance of Folate Trap ?What are the advantages of synthesizing proteases as zymogens?The objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…
- What is the role of a protease? Why is chymotrypsin considered to be a serine protease?Describe type I, II, and III L-asparaginases. Mention characteristics and differences between them with respect to enzyme kinetics (rate, km, etc).Draw the amino acid–Schiff base that forms in the breakdown of 3-hydroxykynurenine to yield 3-hydroxyanthranilate in the tryptophan degradation pathway (Fig.) and indicate which bond is to be cleaved.
- A seven-residue peptide was found to have an amino acid composition including glu, val, Lys, met, leu, and trp (there is more than one copy of one amino acid). Several reactions on samples of the peptide resulted in the following: a) Trypsin has no effect on the heptapeptide. b) If one cycle of Edman degradation provides the PTH derivative shown below, what does this tell you about the oligopeptide under investigation? [image] c) Chymotrypsin treatment yields a dipeptide, a tetrapeptide, and a free amino acid. Possibilities? d) The tetrapeptide contains val, lys, and met (only). What information does this give you? e) Cyanogen bromide treatment generates a dipeptide, a tetrapeptide, and free Lys. f)What is the sequence of the peptide?Which of the following amino acids can act as nucleophiles in a protease active site (choose all that apply): a) Cysteine b) Alanine c) Leucine d) Serine e) ThreonineWhich of the following is a substrate from primase?
- A decapeptide which could resist burns was isolated from an endemic plant from Mt. Mayon. Deduce the amino acid sequence of the decapeptide given the following informations. Mercaptoethanol gave two pentapeptides F1 and F2. Chymotrypsin treatment of F1 releases S and a tetrapeptide (C,K,F,M) while F2 gave a dipeptide (M,S) and a tripeptide (C,F,K) F1 when treated with CNBr released a free homoserine lactone and a tetrapeptide. Trypsin treatment of F1 gave a tripeptide and a dipeptide. F2 treated with carboxypeptidase released free M while with trypsin gave free K and a tetrapeptide.Below is an extract which describes the mechanism of action of aldolase during the cleavage of fructose 1, 6-bisphosphate to produce dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP). Fill in the missing words to complete the extract. Listed here is the pool of words to select from: abstracts, acidic, amine, covalent, hydroxyl, lysine, nitrogen, Schiff base, tetrahedral, water. Ring opening of F1,6BP occurs to render a linear sugar bisphosphate molecule.A __________ residue attacks the carbonyl carbon of F1,6BP. As the carbonyl Oxygen gets a negative charge, a proton is abstracted from the active site _________ amino acid. A _________ intermediate is produced. The active site basic amino acid residue _________ a proton from the lysine. A carbon- __________ double bond forms, producing a protonated Schiff base. At the same time, a solvent proton combines with the released hydroxyl group from C2 to form ________ and leaves the active site. The second active site…How does dithiothreitol (DTT) differ from B-mercaptoethanol (BME) as a reducing agent?