100% satisfaction guarantee Immediately available after payment Both online and in PDF No strings attached
logo-home
Previously searched by you
Previously searched by you
logo
UNE Biochemistry Midterm Exam Questions and Answers 100% Pass $12.49
Add to cart
Quickly navigate to
Preview
  2.  
  3. UNE Biochemistry
  4.  
  5. UNE Biochemistry

Exam (elaborations)

UNE Biochemistry Midterm Exam Questions and Answers 100% Pass
 0 view  0 purchase
  • Course
  • UNE Biochemistry
  • Institution
  • UNE Biochemistry

UNE Biochemistry Midterm Exam Questions and Answers 100% Pass How do most enzymes reduce the activation energy needed to move a reaction forward? - Providing an active site most complementary the transition state An enzyme has a mutation within the substrate binding of the coenzyme needed for c...

[Show more]

Preview 3 out of 17  pages

Document information

  • January 8, 2025
  • 17
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers

Subjects

  • une biochemistry midterm exam questions and answer

Written for

  • UNE Biochemistry
  • UNE Biochemistry

Seller

avatar-seller
EmilyCharlene

Reviews received

Content preview

UNE Biochemistry Midterm Exam
Questions and Answers 100% Pass

How do most enzymes reduce the activation energy needed to move a reaction forward? - ✔✔Providing

an active site most complementary the transition state


An enzyme has a mutation within the substrate binding of the coenzyme needed for covalent catalysis.

Which of the following is likely to result as a consequence of this mutation? - ✔✔The enzyme will not be

able to form the transition state complex


Hemoglobin has the ability to display cooperative binding while myoglobin does not display this binding

kinetic pattern. Which of the following differences between the two proteins accounts for this difference

in binding kinetics? - ✔✔The presence of quaternary structure in hemoglobin


Cleavage of fructose 1,6-bisphosphate to dihydroxy and glyceraldehyde 3-phosphate is achieved by what

class of enzymes? - ✔✔Lyase


Domains are common structural elements that retain a particular function within the protein. Which of

the following is an example of a protein domain? - ✔✔An arrangement of beta strands connected to alpha

helices (BaBaB)


Covalent catalysis is used by many enzymes to cleave peptide bonds. Which of the following amino acids

would not facilitate this type of catalysis? - ✔✔Valine


Which of the following proteins is likely to have quaternary structure? - ✔✔A multimeric protein that

contains multiple peptide chains




EMILY CHARLENE © 2025, ALL RIGHTS RESERVED 1

,What of the following best describes a protein domain? - ✔✔A relatively large pattern a three-

dimensional structure that is recognized across many proteins


Movement of ammonia from an amino acid to an a-keto acid involved a family of enzymes best

categorized as which of the following? - ✔✔Tranferases


A 19-year-old boy is diagnosed with Creutzfeldt-Jakob Disease which is caused by the introduction of an

amyloid fold in the disease-causing protein. The introduction of this fold causes the protein to transition

from a primarily a-helix structure to an aggregate of mostly B-sheets. This change in protein structure

(leading to disease) is best attributed to changes in which of the following? - ✔✔Folding of the secondary

structures


Chymotropsin is a protease that cleaves peptide bonds. It is characterized as which of the following

classes of enzymes? - ✔✔Hydrolases


Which of the following best describes tertiary structure? - ✔✔Interactions between single amino acids

adjacent to one another


Hemoglobin has the ability to display cooperative binding while myoglobin does not display this binding

pattern. Which of the following differences between the two proteins accounts for the difference in

binding kinetics? - ✔✔The presence of quaternary structure in hemoglobin


Changes in the physiological variables listed below can alter the affinity of hemoglobin for oxygen.

Which of the following will lower the affinity of hemoglobin for oxygen? - ✔✔Increase in 2,3

bisphosphoglycerate (BPG)


An enzyme has a mutation within the substrate binding site that reduces the binding of the coenzyme

needed for covalent catalysis. Which of the following is likely to result as a consequence of this mutation?

- ✔✔The enzyme will not be able to form the transition state complex




EMILY CHARLENE © 2025, ALL RIGHTS RESERVED 2

, An enzyme is participating in a general acid-base catalysis reaction with an optimal reaction pH of 6.0. If

acid is added to the environment reducing the pH to 3, what is the likely impact to the rate of reaction? -

✔✔The rate of the reaction is likely to decrease as the pH is out of optimal catalytic range


Which of the following best describes an enzyme inhibitor that increases the Km but does not change the

Vmax? - ✔✔A competitive inhibitor


The association of DNA and histones can be modified by histone acetylation. A decrease in histone

acetylation will have which of the following impacts on the association of DNA and histones? -

✔✔Increase DNA: histone association


In the image below the blue line indicates enzyme kinetics with no inhibitor present. Based on this

information which of the following is true? - ✔✔The green line shows enzyme kinetics with the addition

of a noncompetitive inhibitor


The following represents a series of reactions. As levels of B increase, this will decrease the conversion of

S3 to B. Which of the following best describes this type of regulation in a biosynthetic pathway? -

✔✔Feedback inhibition


Which of the following is an example of enzyme regulation through covalent modification? -

✔✔Phosphorylation of muscle glycogen phosphorylase


Under low energy conditions, AMP will bind to phosphofructokinase 1 and glycogen phophorylase at a

site unique to the active site. This enhances the activity of these enzymes. This is an example of which of

the following types of enzyme regulation? - ✔✔Allosteric activation


A new enzyme is discovered that increases in activity when it is phosphorylated on an exposed tyrosine

residue. Phosphorylation of this amino acid is classified as which of the following? - ✔✔Phosphorylation

is a common covalent modification that can have various impacts on activity




EMILY CHARLENE © 2025, ALL RIGHTS RESERVED 3

The benefits of buying summaries with Stuvia:

Guaranteed quality through customer reviews

Guaranteed quality through customer reviews

Stuvia customers have reviewed more than 700,000 summaries. This how you know that you are buying the best documents.

Quick and easy check-out

Quick and easy check-out

You can quickly pay through credit card or Stuvia-credit for the summaries. There is no membership needed.

Focus on what matters

Focus on what matters

Your fellow students write the study notes themselves, which is why the documents are always reliable and up-to-date. This ensures you quickly get to the core!

Frequently asked questions

What do I get when I buy this document?

You get a PDF, available immediately after your purchase. The purchased document is accessible anytime, anywhere and indefinitely through your profile.

Satisfaction guarantee: how does it work?

Our satisfaction guarantee ensures that you always find a study document that suits you well. You fill out a form, and our customer service team takes care of the rest.

Who am I buying these notes from?

Stuvia is a marketplace, so you are not buying this document from us, but from seller EmilyCharlene. Stuvia facilitates payment to the seller.

Will I be stuck with a subscription?

No, you only buy these notes for $12.49. You're not tied to anything after your purchase.

Can Stuvia be trusted?

4.6 stars on Google & Trustpilot (+1000 reviews)

51292 documents were sold in the last 30 days

Founded in 2010, the go-to place to buy study notes for 15 years now

Start selling
$12.49
  • (0)
Add to cart
Added