Polysaccharides may gel through a variety of differentmechanisms. Which of these statements is FALSE?Select one:O a. Alginate gels through the formation of calcium salt bridgesbetween G-blocksO b. Xanthan gum gels through the formation of hydrophobicinteractions between non-polar regions on the chainO c. Kappa-Carrageenan gels through the formation ofpotassium ion bridges between sulfate groupsO d. High methoxy pectin forms gels at acidic pH values andhigh sugar contents because of a reduction in electrostaticrepulsion and the generation of a strong osmotic attraction.

Carbohydrates are divided into 3 classes monosaccharides, disaccharides, and polysaccharides.…

Answered: Polysaccharides may gel through a…

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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Similar questions

Match the following (draw lines connecting the proteins shown on the left).
1. Researchers isolated a monomeric protein from platelets that has 2 binding sites (A and B) for ADP; Site A's Ka is 157 μM, and Site B's Kd is 2.2 μM. 1.1. A) Which binding site has higher affinity for ADP? B) Briefly justify your answer. C) For this higher affinity site, calculate the standard free energy change for ADP binding. Show your work. 1.2. What concentration of ADP is required to get site A filled in 20% of the proteins? 1.3. Based on this information, sketch a graph of the fraction of site B filled as a function of [ADP].
A solution containing two globular proteins each with a single subunit (one is "large" with a radius of 47 Å and the other is "small" with a radius of 16 A) is applied to a gel-filtration (i.e. size-exclusion) column. What is the most likely outcome? O a The outcome will depend on which protein has the most negative surface charge. O b. The small protein elutes before the large protein. O C. The large protein elutes before the small protein. O d. Both proteins elute together. O e. The outcome will depend on the pH of the solution.
The properties of a side chain can be affected by its microenvironment, or the environment that is in the immediate vicinity. For example, the Lys side chain can become slightly more basic its protonated form can be stabilized by its microenvironment. Which of the following microenvironments do you expect to increase the basicity of Lys? O A microenvironment that is composed of hydrophobic residues. O A microenvironment composed of lipid molecules O A microenvironment composed of positively charged side chains. O A microenvironment composed of negatively charged residues.
Which level of protein structure would be most affected by the following changes... a) mutation from isoleucine to valine b) oxidation of two cysteine sidechains c) PrP (healthy prion protein, mostly a-helical) changes to PrP (infectious form, mostly ß-strand) (more than one answer!) d) increase in pH from 7 to 10
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
Which of the following is NOT correctly paired? cellulose: beta-1,4-glycosidic linkage amylose: alpha-1,4-glycosidic linkage chitosan: alpha-1,4-glycosidic linkage cellubiose: beta-1,4-glycosidic linkage Which is NOT correctly paired?Immersive Reader fibrous protein: spherical alpha helix protein: right-handed coil beta pleated sheet: fully extended peptide chain globular protein: soluble in water
which in is the best method for separating proteins A and B that have the properties below: Protein A: a tetramer of identical 80kDa subunits with a pl of 6.4 Protein B: a monomeric protein with a MW of 80kDa and a pl of 9.2 A.) Anion exchange chromatography at pH 11 B.) Gel exclusion chromatography C.) Cation exchange chromatography at pH 4 D. Cation exchange chromatography at pH 11 E.) SDS-PAGE
(a) 1 Normalized fluorescence 0.8 0.6 0.4 0.2 0 1.7.0- 50 55 OM 0.100 M 0.200 M 0.300 M 0.500 M 1.00 M 2.00 M Where is fully folded protein? • Where is fully unfolded protein? • Where is partially folded protein? 60 A 65 Temp. (°C) 70 75 80 To what does SYPRO orange bind? • Why does fluorescence increase as a function of temperature? • Define a melting temperature for a protein. • Demonstrate how an estimated melting temperature of the protein in zero molar ligand can be determined. • What is the effect of increasing the molar concentration on melting temperature for this protein? Why is melting temperature a useful measurement to make for a protein especially if you are interested in protein aggregation?
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
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. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
Can you hypothesize why a mixtureof (Poly U)+(Poly A) would not stimulate incorporation of14C@phenylalanine into protein?

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