Chapter 2 Flashcards
(20 cards)
Why 20 amino acids?
provide chemical versatility, may have been available for prebiotic reactions, larger amino acids may be too reactive
Hydrophobic amino acids
Glycine, Alanine, Proline, Valine, Leucine, Isoleucine, Methionine, Typtophan, Phenylalanine
Polar amino acids
Serine, Threonine, Tyrosine, Asparagine, Glutamine, Cysteine
Postively charged amino acids
Lysine, Arginine, Histidine
Negatively charged amino acids
Aspartate, Glutamate
Primary structure of a protein
Polypeptide chain
beginning of polypeptide chain
N-terminus
Two parts of a polypeptide chain
repeating part, variable part
Residue
single amino acid within the polypeptide chain
End of polypeptide chain
C-terminus
Secondary structure
3D structure formed by hydrogen bonds
tertiary structure
Complete 3D folding by interactions between R groups
quarternary structure
two or more peptide chains forming subunits
homodimer
polypeptide chains that are the same
heterodimer
polypeptide chains that are different
subunits
proteins composed of multiple polypeptide chains
Peptide bond shape
planar
peptide bond charge
uncharged
dimer
set of two units of a molecule connected by a chemical bond
monomer
molecule or atom that bonds with other monomers to form polymers
