Written by students who passed Immediately available after payment Read online or as PDF Wrong document? Swap it for free 4.6 TrustPilot
logo-home
Exam (elaborations)

WGU C785 Biochemistry Unit Questions with Correct Answers

Rating
-
Sold
-
Pages
58
Grade
A+
Uploaded on
23-10-2024
Written in
2024/2025

WGU C785 Biochemistry Unit Questions with Correct Answers Which level of protein structure is disrupted through the hydrolysis of peptide bonds? Quaternary Tertiary Primary Secondary - Ans:-Primary ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 2/58 The primary structure of a protein is the sequence of amino acids held together by peptide bonds. Peptide bonds are formed by dehydration reactions and disrupted by hydrolysis. A mutation in the beta-hemoglobin gene, which results in the replacement of the amino acid glutamate in position 6 with the amino acid valine, leads to the development of sickle cell anemia. The structures of glutamate and valine are shown below. If the beta hemoglobin gene in a patient with sickle-cell anemia were to be edited so that the valine in position 6 was replaced with a different amino acid, which replacement for valine would be expected to have the best clinical outcome, in theory, for the patient? (Assume the valine can potentially be replaced with any amino acid other than glutamate.) - Ans:-The original amino acid in a healthy patient is glutamate, which is negatively charged. The mutated amino acid is valine, which is non-polar. Valine is causing sickle cell anemia. The best amino acid to replace valine so that the patient is healthy again would be the one most like glutamate, so any negatively charged amino acid. Secondary, tertiary, and quaternary levels of protein structure can all be impacted by exposing a protein to which treatment? Change of a hydrophobic amino acid to a different hydrophobic amino acid ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 3/58 Addition of a reducing agent Placement of the protein in a solution with a low pH Increase in the concentration of the protein in solution - Ans:-Placement of the protein in a solution with a low pH Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen bonds in the backbone of amino acids occur in secondary structure, and both hydrogen bonds and ionic bonds occur in the side chains of amino acids in tertiary structure. An increase in beta-pleated sheet structure in some brain proteins can lead to an increase in amyloid deposit formation, characteristic of some neurodegenerative diseases. What is the primary biochemical process that follows the increase in beta-pleated sheet structure that leads to the development of the amyloid deposits? An increase in glycogen formation in the brain cells ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 4/58 Aggregation of the proteins in the brain Secretion of glucagon, leading to excessive ketogenesis An increase in anaerobic metabolism of glucose in the brain - Ans:-Aggregation of the proteins in the brain This question is describing changes in protein structure. Aggregation occurs when proteins clump together inappropriately, causing plaques like amyloid deposits to accumulate. Which level of protein structure is determined by the sequence of amino acids? Secondary structure Quaternary structure ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 5/58 Tertiary structure Primary structure - Ans:-Primary structure The primary structure of a protein is simply the sequence of amino acids held together by peptide bonds. Which force is most influential in determining the secondary structure of a protein? Hydrophobic effect Disulfide bonding Hydrogen bonding Electrostatic interactions - Ans:-Hydrogen bonding ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 6/58 The secondary structure of a protein is built by hydrogen bonds between the carboxyl groups and amino groups on the backbones of the amino acids. Which amino acid would most likely participate in hydrogen bonds? - Ans:-Amino Acid structure 4 This is a polar, uncharged amino acid due to the OH group on the side chain. Polar, uncharged amino acids containing oxygen or NH groups make hydrogen bonds. Which portion of the amino acid is inside the box? The box is surrounding the section below the Alpha Carbon - Ans:-Side Chain The side chain is the variable group of the amino acid, also called the R group. Every amino acid has the same amino group, carboxylic acid group, and an alpha carbon, but the side chain is different. Which pair of amino acids will most likely interact through hydrophobic forces between their side chains? - Ans:-Both of these amino acids are non-polar and therefore

Show more Read less
Institution
WGU C785 Biochemistry
Course
WGU C785 Biochemistry

Content preview

©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




WGU C785 Biochemistry Unit Questions
with Correct Answers

Which level of protein structure is disrupted through the hydrolysis of peptide bonds?




Quaternary




Tertiary




Primary




Secondary - Ans:✔✔-Primary




Page 1/58

, ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




The primary structure of a protein is the sequence of amino acids held together by peptide bonds.

Peptide bonds are formed by dehydration reactions and disrupted by hydrolysis.


A mutation in the beta-hemoglobin gene, which results in the replacement of the amino acid glutamate

in position 6 with the amino acid valine, leads to the development of sickle cell anemia. The structures of

glutamate and valine are shown below.




If the beta hemoglobin gene in a patient with sickle-cell anemia were to be edited so that the valine in

position 6 was replaced with a different amino acid, which replacement for valine would be expected to

have the best clinical outcome, in theory, for the patient? (Assume the valine can potentially be replaced

with any amino acid other than glutamate.) - Ans:✔✔-The original amino acid in a healthy patient is

glutamate, which is negatively charged. The mutated amino acid is valine, which is non-polar. Valine is

causing sickle cell anemia. The best amino acid to replace valine so that the patient is healthy again

would be the one most like glutamate, so any negatively charged amino acid.


Secondary, tertiary, and quaternary levels of protein structure can all be impacted by exposing a protein

to which treatment?




Change of a hydrophobic amino acid to a different hydrophobic amino acid




Page 2/58

, ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




Addition of a reducing agent




Placement of the protein in a solution with a low pH




Increase in the concentration of the protein in solution - Ans:✔✔-Placement of the protein in a solution

with a low pH




Changes in pH affect hydrogen bonds and ionic bonds. Hydrogen bonds in the backbone of amino acids

occur in secondary structure, and both hydrogen bonds and ionic bonds occur in the side chains of

amino acids in tertiary structure.


An increase in beta-pleated sheet structure in some brain proteins can lead to an increase in amyloid

deposit formation, characteristic of some neurodegenerative diseases. What is the primary biochemical

process that follows the increase in beta-pleated sheet structure that leads to the development of the

amyloid deposits?




An increase in glycogen formation in the brain cells




Page 3/58

, ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED

FIRST PUBLISH OCTOBER 2024




Aggregation of the proteins in the brain




Secretion of glucagon, leading to excessive ketogenesis




An increase in anaerobic metabolism of glucose in the brain - Ans:✔✔-Aggregation of the proteins in the

brain




This question is describing changes in protein structure. Aggregation occurs when proteins clump

together inappropriately, causing plaques like amyloid deposits to accumulate.


Which level of protein structure is determined by the sequence of amino acids?




Secondary structure




Quaternary structure




Page 4/58

Written for

Institution
WGU C785 Biochemistry
Course
WGU C785 Biochemistry

Document information

Uploaded on
October 23, 2024
Number of pages
58
Written in
2024/2025
Type
Exam (elaborations)
Contains
Questions & answers

Subjects

$12.99
Get access to the full document:

Wrong document? Swap it for free Within 14 days of purchase and before downloading, you can choose a different document. You can simply spend the amount again.
Written by students who passed
Immediately available after payment
Read online or as PDF

Get to know the seller

Seller avatar
Reputation scores are based on the amount of documents a seller has sold for a fee and the reviews they have received for those documents. There are three levels: Bronze, Silver and Gold. The better the reputation, the more your can rely on the quality of the sellers work.
GraceAmelia West Virginia University
Follow You need to be logged in order to follow users or courses
Sold
99
Member since
2 year
Number of followers
32
Documents
8971
Last sold
1 month ago
GraceAmelia\'s Emporium

Get a well Researched and Accurate Study Materials to Boost Your Grades and Excel Academically Offered by Seller Grace.

2.8

8 reviews

5
2
4
1
3
1
2
1
1
3

Why students choose Stuvia

Created by fellow students, verified by reviews

Quality you can trust: written by students who passed their tests and reviewed by others who've used these notes.

Didn't get what you expected? Choose another document

No worries! You can instantly pick a different document that better fits what you're looking for.

Pay as you like, start learning right away

No subscription, no commitments. Pay the way you're used to via credit card and download your PDF document instantly.

Student with book image

“Bought, downloaded, and aced it. It really can be that simple.”

Alisha Student

Working on your references?

Create accurate citations in APA, MLA and Harvard with our free citation generator.

Working on your references?

Frequently asked questions