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- Acetylating agents such as acetic anhydride react preferentially with primaryamines, iodoacetate reacts preferentially with sulfhydryl groups (see Tools of Biochemistry 5B), and ATP-dependent kinases preferentially add a phosphoryl group to side-chain hydroxyl or phenolic —OH groups. Which amino acid side chains, or main-chain groups, in a polypeptide are most likely to be modified by treatment with:(a) acetic anhydride(b) iodoacetate(c) a kinase + ATPThe glycosaminoglycan polysaccharide chainsthat are linked to specific core proteins to form the pro-teoglycan components of the extracellular space arehighly negatively charged. How do you suppose thesenegatively charged polysaccharide chains help to estab-lish a hydrated gel-like environment around the cell? Howwould the properties of these molecules differ if the poly-saccharide chains were uncharged?Consider a hexapeptide of the sequence thr asn glu trp lys gln. After complete hydrolysis, which amino acid would elute first from a cation exchange column at pH 7? O Asn O GIn Thr Glu O Trp O Lys
- Draw the structure of phosphatidylcholine at pH 7 with the moiety on R₁ as 14:0 (C14) and R₂ as 12:2cis,cis-A6,9. Put an X on the bond cleaved by Phospholipase C.What is the difference between an enol phosphate and a normal phosphate ester that gives PEP such a high phosphoryl group transfer potential?The anomer of a-D-glucopyranose is CH:OH он ÓH CH2OH он он он он CH,OH он он он он CH,OH он OH он ÓH ÇH;OH он он он он
- Collagen is unusual in its amino acid composition and requires a wide variety of posttranslational modifications to convert it to a functional molecule. Because of the complexity of collagen synthesis, there are many diseases, resulting in structural weaknesses in connective tissue, caused by defects in the process. Scurvy leads to a less stable collagen lacking sufficient hydroxyproline. 4-Hydroxylation of specific prolyl residues during collagen synthesis requires all of the following except A. Fe2+ B. a specific amino acid sequence at the site of hydroxylation. C. ascorbic acid. D. co-hydroxylation of lysine . E. individual α-chains, not yet assembled into a triple helix.Starting from glutamine ,glycine, aspartate, N-10 formal-ThF ,how many ATP equivalents are required for purine synthesis?Predict the locations of 14C in Aspartate synthesis using the following labeled 14C succinate. -OO14C-CH2-14CH2-14COO-
- Which of the following statements about sugar polymers and glycosaminoglycans is/are true? Glucosamine, an amino sugar, would be positively charged physiologically unless it is part of an amide bond. Chitin is a homopolymer of GlcNac in beta 1--> 4 linkages. Amylose is a homopolymer of glucose containing alpha 1--> 6 linkages. Amylopectin in a non-reducing sugar polymer consisting solely of glucose monomers. Agarose is a highly charged sugar polymer used in electrophoresis. A core of hyaluronan protein is linked to an aggrecan polysaccharide in the extracellular matrix around joints and tendons. Mucins are secreted proteins that contain branched oligosaccharides linked to serine residues. None of the options shown is true. The glycosaminoglycan "hyaluronic acid" would carry more negative charge overall when compared to a polymer of "chondroitin" of the same length. Please answer very soon will give rating surely Complete Answer neededDraw the first tetrahedral intermediate of the chymotrypsin mechanism (a single structure, no arrows required). Circle the oxyanion hole. How does the oxyanion hole of chymotrypsin compare to that of carboxypeptidase?draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). H;N+- CH - COOH (CH2)4 NH3+