Study your flashcards anywhere!

Download the official Cram app for free >

  • 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

How to study your flashcards.

Right/Left arrow keys: Navigate between flashcards.right arrow keyleft arrow key

Up/Down arrow keys: Flip the card between the front and back.down keyup key

H key: Show hint (3rd side).h key

A key: Read text to speech.a key


Play button


Play button




Click to flip

15 Cards in this Set

  • Front
  • Back
proteins with more than one subunit
consists of one pp chain or several unlike pp chains
What is considered a protein's quaternary structure?
the spatial arrangement of a macromolecule's individual subunits
What is the only type of symmetry that proteins can have?
What is hydropathy?
the combined hydrophobic and hydrophilic tendencies of individual amino acid residues in proteins
A larger hydropathy makes what more likely?
for the residue to occupy the interior of the proein

Hydrogen bonds make only minor contributions to protein stability.
For what are H-bonds important in proteins (considering quaternary structure)
important determinants of native structure
ion pair/ salt bridge
association of 2 ionic protein groups of opposite charge
Why is Zinc ideal for the structural role in intracellular proteins?
-its filled d electron shell permits it to interact strongly with a variety of ligands (sulfur, nitrogen, oxygen)
-has only one stable oxidation state and so does not undergo oxidation-reduction in the cell
What is a ligand?
1. a small molecule that binds to a larger one

2. a molecule or ion bound to a metal ion
In what geometry are Zinc fingers coordinated?
What is breathing?
the small conformational fluctuations of a protein molecule
What are chaotropic agents?
ions or small organic molecules that increase the solubility of nonpolar substances in water
What did Anfinsen's work on ribonuclease A (RNase A) show?
proteins can fold spontaneously into their native conformations under physiological conditions---- A PROTEIN'S PRIMARY STRUCTURE DICTATES ITS 3-D STRUCTURE