• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/11

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

11 Cards in this Set

  • Front
  • Back
Which interaction is the major driving force of protein interactions/folding?
Hydrophobic interactions
What is the order of strength of bonds seen in cells?
Covalent > ionic > H bonds > van der Waals attractions
Give an instance of covalent bonding in protein folding. Under what conditions must this occur?
Disulfide bonds formed between cysteine a.a.'s. Formed under oxidizing conditions.
Where would you see disulfide bridges forming?
In the secretory pathway (i.e.: ER, golgi, endosomes, lysosomes, extracellular space, etc.)
Where won't you see disulfide bridges in proteins?
In the cytosol, the nucleus or mitochondria.
What designates the formation of secondary structures of amino acids?
H-bonds.
What drives the formation of tertiary structures in proteins? Where, specifically?
Hydrophobic interactions between the side chains (R chains).
Define a domain.
A self-contained folded unit of a polypeptide.
Most polypeptides are ____ to ____ amino acids long.
100-800
What is the weight range of the average polypeptide?
12 to 90kDa of molecular weight.
Native states can be in equilibrium with near-native states (ie. molten globules). True or False?
True.