Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of twoglycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein,the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to theglycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3)bond also to three sialic acid residues, then also O-linked to the glycoprotein.Function of 1st glycoprotein – glucose transporter proteinFunction of 2nd glycoprotein – Na*-K* receptor/ transporterWhy is there a difference in the functions of the two glycoproteins?

Glycoproteins are consisted of protein and glycan moiety which is involved in several biological…

Answered: Saccharide X, a sugar composed of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein, the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3) bond also to three sialic acid residues, then also O-linked to the glycoprotein. The saccharide was cleaved from its sialic acid residues. The treatments and results are as follows: 1. hydrolysis by B(1-> 4) - disaccharide products 2. hydrolysis by a(1-> 4) - release of 2 disaccharide & 2 monosaccharide units. Show the structure of the saccharide.
Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of a glycoprotein. The saccharide is linked by a(1-2) linkages to three sialic acid residues, then O- linked to the glycoprotein. The glycoprotein is a glucose receptor. Running it through Benedict's Test produced negative results. What are 2 possible amino acids that is able to O-link with the saccharide? Show the part of both saccharide and protein where the bond is formed.
All sugar residues are in their D-isomeric forms. What kind of glycosidic linkage is between the first and second residues? What kind of glycosidic linkage is between the third and second residues?
Saccharide M, a sugar made of repeating units of maltose and cellobiose, is a component of glycoproteins 1 and 2, which are receptors found in the membrane of Shrek's cells. For glycoprotein 1, saccharide M is attached by an a 1® 2 linkages to 3 sialic acid residues, then O-linked to the protein, while glycoprotein 2 has saccharide M attached by a b 1®3 bond also to 3 sialic acid residues, then it is also O-linked to the protein. Glycoprotein 1 is a transporter protein for glucose, while glycoprotein 2 is the Na*-K*receptor/ transporter. The glycoproteins show 99% sequence homology of its amino acid sequence. a. Explain briefly why there is a difference in the functions of glycoprotein 1 and 2 b. Glycoprotein 1 is a receptor for glucose. Using Benedict's reagent, tests on the glycoprotein gave NEGATIVE results. Give 2 amino acids that can O-link with Saccharide M and show the portion of both protein and saccharide where a bond will be formed.
The endorphins are a group of naturally occurring neurotransmitters that act in a manner like morphine to control pain. Research has shown that the biologically active parts of the endorphin molecules are simple pentapeptides called enkephalins. Draw the structure of the methionine enkephalin with the sequence Tyr-Gly-Gly-Phe-Met. Identify the N-terminal and C-terminal amino acids. Bradykinin is a nonapeptide that stimulates smooth muscle contraction, dilates blood vessels, causes pain, and is a component of bee venom. Give the IUPAC name of the nonapeptide. Note: The selected photo is the sequence of Bradykinin.
An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?
Heparin, a highly negatively charged glycosaminoglycan, is used clinically as an anticoagulant. It acts by binding several plasma proteins, including antithrombin III, an inhibitor of blood clotting. The 1:1 binding of heparin to antithrombin III seems to cause a conformational change in the protein thatgreatly increases its ability to inhibit clotting. What amino acid residues of antithrombin III are likely to interact with heparin?
Chondroitin sulfate chains have been likened to a large fishnet, allowing small molecules to pass through but excluding large ones. What structural features of chondroitin sulfate and proteoglycans in general are responsible for this phenomenon?
Why is B-D-Glucopyranose in a chair conformation form is the most stable form of glucose present in our body?
Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…
Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln 8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…
Histidine is an amino acid containing an ionizable group in its side chain. This ionizable group has a pka of 6.0, meaning that His is in its deprotonated form at physiological pH (7.0-7.4). However, His is included in the positively charged amino acid category. Calculate the ratio of deprotonated/protonated His at pH 7.0, and use your answer to justify why this amino acid is included in the positively charged amino acid category. Show all work for full credit.

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