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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Similar questions

The elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a change in pH from 7.4 to 6.9 in which type of protein separation technique? a.) size exclusion chromatography b.) SDS-acrylamide gel electrophoresis c.) affinity chromatography d.) ion exchange chromatography
Which of the following statements are true about stacking and separating gels? a. The holes is the separating gel are much smaller than the ones in the stacking gel. b. The stacking gel is at a pH of 6.9, while separating gel is at a pH of 8.9 c. The higher pH in separating gel causes the glycine buffer to accelerate more and thus leaving behind the proteins to stack at the interface. d. The smaller holes in separating gel slows down the mobility of the proteins at the interface.
Explain the changes that you observed in terms of change in protein structure at the molecular level of egg albumin Hint: Discuss what interactions/bonds are disrupted upon application of the treatment on the egg albumin during denaturation Heat Vinegar Rubbing alcohol
Which of the following does not describe protein modifications? please explain the answer a.They can promote multiprotein complex formation b.They can target a protein for proper localization c.They can regulate protein stability d.They are always permanent changes
Rationalize the following observations.(a) Serine is the amino acid residue that can be replaced with theleast effect on protein structure and function.(b) Replacement of tryptophan causes the greatest effect on protein structure and function.(c) Replacements such as Lys -> Arg and Leu -> Ile usually havevery little effect on protein structure and function.
In the protein denaturation experiment, which of the following can be a consequence of the air bubbles in the viscometry run for an aqueous solution of protein with a denaturant?a. Increased t0b. Decreased t0c. Increased nspd. Decreased nspAll of the statements about protein denaturation are true EXCEPT:a. The viscosity of linear proteins is greater than that of the globular proteins.b. Only the BME can disrupt a covalent bond while the other denaturants can just disrupt non-covalent bonds.c. Protein renaturation is possible but in some cases protein denaturation proceeds to protein degradation. d. Protein denaturation generally disrupts tertiary or quaternary structures only
When a protein is denatured using heat Select one: a. its C-terminal will change. b. its tertiary structure will change. c. its amino acid sequence will change. d. its amino acid composition will change.
SDS coats proteins with a: A) Positive Charge B) Negative Charge
Which of the following explains why beta sheets are the secondary structures observed in aggregates? a. Beta sheet structures can form between differing peptide chains allowing for aggregates b. This is a false statement; aggregates prefer fibrous structures like tropocollagen c. Beta sheet structures are formed with lots of charged residues that form ionic interactions to further stabilize the structure of the aggregate d. Beta sheet structures contain numerous cysteinyl residues that allow for formation of disulfide bonds for stabilizing the aggregate
Indicate which of the following are present in the primary, secondary, tertiary, and quaternary structures ofproteins: a. peptidebonds b. hydrogen bonds between adjacentpeptides c. hydrogen bonds within a singlepeptide d. hydrophobic interactions e. association of four polypeptide chains
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
Proteins denature at low pH. What characteristic of acidic environments interferes with protein folding? A. The lack of protons in the solution breaks covalent bonds in the protein. B. The excess protons in the solution break covalent bonds in the protein. C. The lack of protons in the solution breaks hydrogen bonds in the protein. D. The excess protons in the solution break hydrogen bonds in the protein.

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