Amino Acids and Proteins Flashcards
3 Major Groups of Amino Acids
-non-polar
-polar
-electrically charged amino acids
2 types of electrically charged amino acids
acid and base
end of amino acid that has an unbound amino group
amino terminus (N-terminus)
end of amino acid that has unbound carboxyl group
C-terminus
peptide bond
bond between the C in the COOH of one amino acid and N in the NH2 of the next amino acid
primary structure
-sequence of amino acids in a polypeptide chain determined by gene that encodes for that protein
Secondary structure
- a helix
- B pleated sheets
H bonding of the peptide backbone causes the amino acids to fold into repeating pattern
a helix
-often on the exterior of protein and involved in interactions with other molecules
-H bonds between every 4th amino acid
common types of tertiary interactions
- Hydrophobic interactions: amino acids with nonpolar, hydrophobic R groups cluster together on the inside of the protein, leaving hydrophilic amino acids on the outside to interact with surrounding water molecules.
- disulfide bridges: - covalent linkages between the sulfur-containing side chains of cysteines
- act like molecular “safety pins,” keeping parts of the polypeptide firmly attached to one another
protein consisting of more than 1 amino acid chain
quarternary structure
Ways to Represent a Protein
- ribbon model of lysozymes
- space-filling model of lysozyme
ribbon model of lysozymes pros and cons
Pros
- very good at showing the secondary structure
- show functional units of protein
Cons
-can’t show us a realistic representation of what this protein looks like