Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of aglycoprotein. 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'sTest produced negative results. What are 2 possible amino acids that is able to O-link with thesaccharide? Show the part of both saccharide and protein where the bond is formed.

Plants constitute a large number of carbohydrates. Glycobiology means the study of the…

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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Lactose permease, a protein of E. coli, is composed of a singlepolypeptide that is 417 amino acids in length. By convention, theamino acids within a polypeptide are numbered from the aminoterminalend to the carboxyl-terminal end. Are the following questionsabout lactose permease true or false?A. Because the sixty-fourth amino acid is glycine and the sixty- eighth amino acid is aspartic acid, the codon for glycine,64, is closer to the 3′ end of the mRNA than the codon for aspartic acid, 68.B. The mRNA that encodes lactose permease must be greater than1241 nucleotides in length.
Consider a mutation that results in a substitution of Cysteine (CYS) ) for Tyrosine (TYR) at position 368. What are the properties of the substituted amino acid, CYS? Does it have any special properties?
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.
Which of the following is an example of an unacceptable missense? a. HbA is converted to Hb Hikari, where the beta chain Lysine at #61 is replaced by Asparagine. b. Hb A, is converted to Hb M (Boston) where the alpha chain Histidine at #58 is replaced by Tyrosine. c. Hb A is converted to Hb S, where the beta chain Glutamate at #6 is replaced by Valine.
Here is a putative peptide sequence (position number on top of residues): 1 2 3 4 5 6 7 8 9 10 11 12 13 NH2- G C G N V T H N Q C V L S -COOH If expressed in a eukaryotic cell (please mark your answer in the blank space): Position(s) ___ could be N-glycosylated Position(s) ___ could be modified with myristic acid and the bond formed would be a ______________ Position(s) ______and _____ could be modified with palmiti c acid and the bond formed would be a ______________ Positio n(s) ________ could be a segment of a lipid-linked protein with a farnesyl anchor and the bond formed would be a ______________ Position(s) ________ could be a segment of an O-glycosylated protein Position(s) ________ could be modified with a glycosylphosphatidylinositol (GPI) anchor Position(s) ________ could be phosphorylated
When the amino acid sequences of insulin isolated from differentorganisms were determined, some differences were noted.For example, alanine was substituted for threonine, serine wassubstituted for glycine, and valine was substituted for isoleucineat corresponding positions in the protein. List the single-basechanges that could occur in triplets to produce these amino acidchanges.
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?
When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?
Many eukaryotic enzymes, such as fatty acid synthase, are multifunctional proteins with multiple active sites covalently linked. What is the advantage of this arrangement?
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?
The enzyme phosphoglucomutase interconverts glucose-1-phosphate and glucose-6-phosphate. Why is this enzyme likely to include a side chain such as Ser in its active site?
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?

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