Lecture 1 - Amino Acids, Peptides, and Proteins

catalysis (enzymes), transport, structure, and motion

the 4 main functions of proteins

DNA polymerase and RNA polymerase

2 examples of proteins involved in catalysis

hemoglobin, myoglobin, and lactose permease

3 proteins involved in transport

collagen and keratin

2 proteins involved in structure

myosin and actin

2 proteins involved in motion

capacity to polymerize, acid-base properties, physical properties, and chemical functionality

4 properties of amino acids that make them well-suited to carry out a variety of biological functions

carboxyl group, amino group, chiral center, hydrogen, and R side chain

general structure of an amino acid

proline (cyclic amino acid)

which amino acid is an exception to the general structure of an amino acid

glycine

which amino acid is not chiral

L

proteins only contain ___ amino acids

1. nonpolar aliphatic (7)

2. nonpolar aromatic (3)

3. polar uncharged (5)

4. polar positively charged (3)

5. polar negatively charged (2)

the 5 basic groups amino acids are placed in

glycine, alanine, proline, valine, leucine, isoleucine, and methionine

nonpolar aliphatic amino acids

phenylalanine, tyrosine, and tryptophan

nonpolar aromatic amino acids

serine, threonine, cysteine, asparagine, and glutamine

polar uncharged amino acids

cysteine

which amino acid can form disulfide bonds

lysine, arginine, and histidine

polar positively charged amino acids

aspartate and glutamate

polar negatively charged amino acids

ampholytes

aminos acids that can act as an acid or base

post-translational modifications

how do uncommon amino acids in proteins arise

kinase

enzyme responsible for phosphorylation

phosphatase

enzyme responsible for dephosphorylation