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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Consider the peptide Asp-Lys-Phe-Glu-Asn-Tyr-Gln-Val-Cys. In a single beaker, you treat this peptide with 2 proteases. One protease cleaves at the N-terminus of aromatic R groups and the other cleaves at the C-terminus of polar, non-ionizable R groups. Following the enzymatic digestion, you want to separate your peptide fragments so that you can identify them. You choose to separate the fragments using an anion exchange column. Beginning at pH=6 you apply your peptide fragments to the column and you gradually decrease the pH of the column stopping the separation when the pH of the column equals 4. Omitting chemical structures, write the amino acid sequence of the peptide fragments that are produced from this digest. Write the order that these fragments will elute from the column (if at all). (Relevant pKa values are: 2.1, 3.8, 4.3, 8.3, 9.6, 10.1, and 10.5)
The core of pectin molecules is a polymer of α (1->4)-linked D-galacturonate. Draw one of its residues.
(iii) Draw a structural diagram of a hydrogen bond between β-D-glucose and the side chain of any polar residue in a protein. (iv) Name the type of bond that can occur between the axial hydrogens of glucose and the indole ring of tryptophan. Draw a structural diagram of this bond. (v) Comment on the polar / apolar nature of the bond in part (iv) and explain why this type of interaction is prevalent in protein-sugar complexes. Answer (iii) to (v) please.
Most animals cannot use wool for nourishment. An exception is the clothes moth: it can derive nourishment from eating clothing made of natural fibers such as wool (which is rich in a-keratin). The digestive tract of the larvae of clothes moths provides a highly reducing environment. Why is this beneficial to the larvae? The reducing environment will reduce the disulfide linkages, making it easier to digest the proteins. The reducing environment will hydrolyze the peptide bonds. The reducing environment will interfere with the H-bonding between the tropocollagen molecules, making the type of protein found in most natural fibres easier to digest. The reducing environment will help to kill bacterial pathogens. The reducing environment will detoxify the carcinogenic dyes used in the textile industry.
Draw the formula of each of the following: a. Aspartic acid-histidine-tryptophan b. Glycine-cysteine-tyrosine with the charges that exist in cell fluid.
Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.
A cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.
The tetrapeptide Cys-Trp-Lys-Pro was digested with chymotrypsin and adjusted to pH=0.5 to fully protonate all digestion products. The digestion products were then applied to a strong cation exchange column (sulfonic acid). The products were eluted from the column using a pH gradient from 0.5 to 13. Write the primary amino acid sequence of the products in the order they would elute from the column. Indicate the pH value at which each product elutes from the column
A peptide with endorphin-like property was produced and obtained from the blood. This was sequence using the protocol: Treatment with streptococcal protease gave a tripeptide and a tetrapeptide. Treatment with trypsin gave two tripeptides and an amino acid. Treatment of the 2 tripeptide products in 1.2 with 2,4-dinitrophenol gave DNP- S, and DNP-E and a mixture of amino acids. The composition of the peptide is G, E, S, and K in a 2:1:1:3 molar ratio. a. Determine the sequence of the peptide? b. Determine the pl and position in an electrophoretic profile
All naturally occurring polysaccharides have one terminal residue, which contains a free anomeric carbon. Why do these polysaccharides not give a positive chemical test for a reducing sugar?Please explain
Are all the amino-acids soluble in water? Explain why?
Describe the chemical difference between mannose and heptyl alpha-D-mannose. Why does FimH have a higher affinity for heptyl a-D-mannose versus methyl a-D-mannose?

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