Which of the following is MOST likely the reason whyprions are infective?A. Prions are small proteins that can easily bind to allostericsites of other proteins causing steric and electrostaticrepulsions that affect protein structure.B. Prions mediate protein foldingC. Prions have exposed hydrophobic cores capable ofinteracting with non-polar groups in proteins which it alsoalters for maximum interactions.D. Prions increase thermodynamic instability of externalresidues by disrupting H2O-protein interactionsE. Prions are small proteins that inhibits folding of proteinsto its proper conformation

Prions are a specific type of protein that triggers normal proteins in the brain to fold abnormally.

Answered: Which of the following is MOST likely…

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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Define the following terms: a. phosphoryl group transfer potential b. adenosine c. adenosine monophosphate d. high-energy bond e. resonance hybrid
One approach to combat drug resistance in bacteria is to combine drugs to treat bacterial infections. For example, ampicillin, a beta-lactam antibiotic, is combined with clavulanic acid, a beta-lactamase inhibitor. Describe how these two drugs would act together to be more effective to treat a bacterial infection.
A structural difference between uracil and cystosine is: A. At C-4 cytosine has an amino group, while uracil as an oxo group B. At C-6 cytosine has an amino group, while uracil as an oxo group C. At C-4 cytosine has an amino group, while uracil as an oxo group D. Both have an oxo group at C-2 E. At C-2 cytosine has an amino group, while uracil as an oxo group
6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.
Sketch a plot that shows a typical binding curve for the interactions between a ligand, L (in terms of concentration), and a protein, P.
A patient is suffering from hemoglobinopathies and the principal biochemical defect that leads to the development of Hb c involves the substitution of at the sixth position of the b-polypeptide chain: a. Proline replaced by cysteine b. Phenylalanine replaced by lysine c. glutamate replaced by Lysine d. glutamic acid replaced by alanine ->
Which factors will cause protein denaturation? Group of answer choices a. aqueous phosphate buffer b. heavy metals - Hg2+, Pb2+, Ag+ c. small metal ions - Na+, Ca2+, Cl- d. changes in pH e. use of detergents or soaps f. Tris a buffer commonly used with proteins
Our body is compost of about 70% water which means that majority of the chemical happens in aqueous medium. Of the residues of the following amino acids: methionine, histidine, arginine, phenylalanine, valine, glutamine and glutamic acid, which would you expect to find a. on the surface of a protein b. in the interior processes
All of the following are ways of controlling enzyme mechanism, except A. Edman degradation B. zymogens C. phosphorylation D. allosteric
The activity of a cellular enzyme could be transiently altered by which of the following modifications to the enzyme? A. Phosphorylatin at serine or tyrosine residues B. Attaching fatty acid groups C. N-terminal acetylation D. Hydroxylation of proline and lysine residues E. Proteolytic cleavage of a peptide fragment
Which of the following is incorrect about chymotrypsin, trypsin, and elastase? a. They catalyze the hydrolysis of the peptide bond b. They have similar amino acid sequences and tertiary structures c. None; all the other choices are correct Od. They have different substrate binding sites
Which of the following statements are correct about the thermodynamics of protein folding (select all that appy)? A. The deltaG for protein folding is negative B. Burial of hydrophobic side provides a positive entropy change that drive protein folding C. The overall entropy change of protein folding is favorable D. Intercations between amino acids provide a large negative deltaH that helps favor the native state. E. The free energy change of protein folding is dependent on the temperature

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