• 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

1/13

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;

13 Cards in this Set

  • Front
  • Back

what makes one amino acid different from another amino acid

The R (residue) group differs with each amino acid.

What is the pKa of an amino acid

The pKa is the pH at the inflection point where the slope is very shallow. pKa is the pH where is concentration of the deprotonated form equals the concentration of the protonated form. At the pKa, buffering capacity is optimal and thus changes in the pH due to the addition of acids and bases are resisted - a shallow slope.

zwitterion

a zwitterion is a form of molecule which carries both a positive an negative charge, it occurs at a pH value between the pKa values of the ionizable group.

What is the isoelectric point

pH value at which the number of positive charges equals the number of negative charges. tied to the zwitterion being in the middle.

polypeptide

a polypeptide is a chain made of more than 50 amino acids.

oligopeptide

chain made of 3-50 amino acids

Primary structure

the covalent linear structure of the protein that is specified by its amino acid sequence as determined by the genetic code.

Secondary structure

localized regular, repitive folding patterns; alpha helix and beta pleated sheets .

Tertiary structure

refers to the overall 3D folding pattern of the polypeptide; creates binding sites and situates R groups in the appropriate environment.

Quaternary structure

formed by the interactions between different polypeptide chains, known as subunits; results in increased protein structure and the possibility of cooperativity for ilgand binding.

ligand

molecule that binds to a binding site on a protein.

prosthetic group

a coenzyme or metal ion that is very tightly or even covalently bound to the enzyme protein is called the prosthetic group. in absence of the prosthetic group, the polypeptide component is known as an apoprotein; in its presence, known as a holoprotein.

2 ways proteins can be denatured

acid and heat