Exam (elaborations)
MCBM 1- (3) Amino Acids, Peptides, and Protein Structures Questions with 100% Correct Answers
- Course
- Institution
MCBM 1- (3) Amino Acids, Peptides, and Protein Structures Questions with 100% Correct Answers
[Show more]
Content preview
1 of 21Term
Discuss peptide bonds. What specifically is reacting with what? What
is the reaction called? What is a byproduct? What are the ends
called?
Give this one a try later!
Loose domain formations --> high density protein formation
Two or more domains included.
, After this process, proteins have acquired final structure and FULL
function. An example of this would be a catalytic domain being able to
function if a substrate binding domain is near it.
They stabilized by hydrogen bonds between peptide strands.
Intrachain=same peptide chain
Interchain=different peptide chains
Parallel strands have N and C termini on the same side, anti parallel
have them on different sides.
Formed by an alpha carboxyl and alpha amino group via
condensation reaction. Water is a byproduct to form a peptide
bond. End is called N or C terminal dependent on whether it is a
carboxyl or amino group.
1) Energetically favorable to avoid contact with water and the
hydrophobic groups.
2) The resulting hydrophobic interactions stabilize the structure, but
not by much.
3) Initial shape formation.
HYDROPHOBIC EFFECT IS THE MOST IMPORTANT FACTOR IN
INITIAL PROTEIN FOLDING!
Don't know?
2 of 21
Term
, Discuss the location of nonpolar and polar amino acids in soluble
and membrane proteins.
Give this one a try later!
Acidic and basic side chains found in the active site of an enzyme.
Triad typically has an acidic, basic, and nucleophilic component.
Acidic side chain has a negative charge, and is responsible for aligning
and polarizing the basic molecule.
The polarization of the basic amino acid helps de-protonate the
nucleophilic amino acid and makes it very reactive.
In a linear soluble protein, nonpolar amino acids aggregate in
the interior of, polar amino acids aggregate on the surface.
In a membrane protein, nonpolar amino acids aggregate on the
surface (in contact with the hydrophobic tails of the bilayer).
Polar amino acids are in contact with the cellular and extra
cellular matrix.
1) Energetically favorable to avoid contact with water and the
hydrophobic groups.
2) The resulting hydrophobic interactions stabilize the structure, but
not by much.
3) Initial shape formation.
HYDROPHOBIC EFFECT IS THE MOST IMPORTANT FACTOR IN
INITIAL PROTEIN FOLDING!
Binding site either forms hydrogen or ionic bonds with the substrate.
The binding site needs to be complementary to the substrate. This is
the very basis of binding specificity.
The benefits of buying summaries with Stuvia:
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
You can quickly pay through credit card or Stuvia-credit for the summaries. There is no membership needed.
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 codersimon. Stuvia facilitates payment to the seller.
Will I be stuck with a subscription?
No, you only buy these notes for $10.00. You're not tied to anything after your purchase.
Can Stuvia be trusted?
4.6 stars on Google & Trustpilot (+1000 reviews)
81113 documents were sold in the last 30 days
Founded in 2010, the go-to place to buy study notes for 14 years now