01. Molecular Structures — RNA & Proteins Flashcards

1
Q

What are some secondary conformations of RNA?

A
  • RNA molecules typically fold onto themselve; complementary sequences within strands
  • G;U — non-Watson-Crick base pairing is possible
  • Stem-loops and hairpin loops can form as a result:
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are some tertiary conformations of RNA?

A
  • Triple base pairing
  • Coaxial rotations around non-base paired segments
  • Pseudoknots around non-adjacent complementary regions
  • A-minor, tetraloop
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are some R-group properties?

A
  • Enzymatic activity
  • Charges
  • H-bonding
  • Modification sites
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are the primary, secondary, and tertiary/quaternary structures of proteins?

A
  1. Polypeptide
  2. Alpha-helix or beta-pleated sheet
  3. Protein
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Describe some posttranslational protein modifications. (Aside from ubiquitination).

A
  • Phosphorylation
    • Regulatory
    • Transient removal or addition of a Pi to an enzyme (activation purposes)
    • Kinases — add Pi to the enzyme
    • Phosphorylase — transfers it back to ATP
  • Sulfation
    • Permanent
  • Acylation
    • Addition of acetyl group to N-terminus
  • Glycosilation
    • Addition of various sugars
    • Useful for identification on cell surface
  • Methylation
  • Prenylation
    • Addition of fatty acids
  • Vitamin C-Dependant
  • Vitamin K-Dependant
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Describe ubiquitination.

A
  • Ubiquitin protein is covalently added to a protein.
  • Can mark it for transport (mono) or proteolysis (poly).
  • Helps regulate protein stability.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly