Explain question 5. Show work how to do it 5. Oligosaccharides structures cover surfaces of cells serving the purpose of recognition byother cells, but also as entryway for bacterial and viral pathogens. These processes usehighly specific recognition enabled by a high diversity of structures generated from theavailable monosaccharide building blocks. Using glucose and mannose only (shownbelow), how many disaccharide structures can be formed? Please, disregard the possibilityof -and-configurations at the reducing end only.dA. 128B. 2C. 5D. 64E. 18HOHOOHOHOne of the availableforms of glucoseOHOHHOSizHOHO.One of the availableforms of mannoseOH6. Despite the fact that amylose and cellulose are both polymers of glucose, they are polaropposites in terms of their three-dimensional structure, their function in biology andapplications. Choose a FALSE statement.A. Cellulose is a linear polymer of -1,4-linked glucose.B. Amylose is a linear polym of -1,4-linked glucose.AC. Cellulose can be readily detected by an intense a dark-blue color it gives by treatmentwith iodine.

Combining glucose (1) and glucose (2) without differentiating the reducing end configurations, we…

Answered: Explain question 5. Show work how to do…

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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I'm conducting an experiment concerned with the binding affinity of tretinoin (all trans retinoic acid) and beta lactoglobulin. This can be accomplished by monitorization of fluorescence quenching of a tryptophanyl residue that resides in a hydrophobic pocket known as a calyx inside the protein. Generally, fluorescence quenching is classified as static or dynamic. Would fluorescence quenching be a result of amide bond formation to tryptophan from tretinoin or through another mechanism (ie FRET: Forester resonance energy transfer)? Could it be both?
I. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?
What structural features make glycans good cell-surface markers? What are the main challenges to glycan analysis? (These challenges are related to the reason why glycans are such good candidates for cell surface recognition elements)Briefly describe the research for which Carolyn Bertozzi was awarded the Nobel prize.
Discuss three polysaccharide structural features that promote gel formation
How many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.
eading list Cells have oligosaccharides displayed on their cell surface that are important for cell-cell recognition. Your friend has discovered a transmembrane glycoprotein, GP1, on a pathogenic fungal cell that is recognized by human immune cells. He decides to purify large amounts of GP1 by expressing it in bacteria. To his purified protein he then adds a branched 14-sugar oligosaccharide to the asparagine of the only Asn-X- Ser sequence found on GP1. Unfortunately, immune cells do not seem to recognize this synthesized glycoprotein. What's a likely explanation for this problem? O The oligosaccharide needs to be further modified before it's mature. O The oligosaccharide should've been added one sugar at a time. O The oligosaccharide needs a disulfide bond. O The oligosaccharideehould've been added to the serine instead of the asparagine.
7. 1 B e here to search Required Study the two diagrams below. Diagram A 2 1 Diagram B 2 Based on the sequence of steps (1, 2, 3), which of the diagrams shows what would happen to proteins made at the ribosomes and transported to the outside of the cell? Diagram A Diagram B Both Diagram A and Diagram B Neither Diagram A nor Diagram B DELL 40)
Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (c) Outline how you would investigate whether BCMAP would be an effective inhibitor for the protein in competition with the molecules that the protein normally targets, and any solvent. Figure 1. 4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and brown, respectively) in the active site of the protein structure.
Given the description of four different proteins above: Which protein will have the highest mobility in an SDS-PAGE gel?
On an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.8 cm, the mobility of the protein is 40 4 40% 0.4
What is the function of sodium dodecyl sulfate (SDS) in SDS-PAGE? stabilizes the gel matrix, improving resolution during electrophoresis SDS solubilizes proteins to give them uniformly negative charges, so the separation is based purely on size. SDS raises the pH of the gel, separating multiunit proteins into individual subunits. SDS solubilizes proteins to give them uniformly positive charges, so separation is based purely on pH.
One of the members of your research group attempted to isolate theenzyme using the protocol you presented. To confirm whether theygot the protein, SDS-PAGE was performed and the gel on the rightwas obtained. Perform the necessary calculations to determine themolecular weight of the suspected band on the gel in the lanelabeled “dialyzed.”

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