Amino acids are made of a carboxyl group, an amino group, and a side group.

The side group will dictate function of the aa, as well as classification.

at a pH of 7.4, the carboxyl group will dissociate and the amino group will become protonated

GAVLIPPTM

Glycine-Alanine-Valine-Leucine-Isoleucine-Phenylalanine-Proline-Tryptophan-Methionin

1. Have no charge

2. Promote hydophobic interactions by moving R group inside protein

3. Found on outside of protein membranes, interacting with lipids

Cysteine-Threonine-Glycine-Asparagine-Tyrosin-Serine

(Sisters and Three GATS)

Have a zero net charge and can participate in H bonds

Also serveas attachment sites for phosphates and oligosaccharides

Asparctic Acid

Glutamic Acid

Histidine

Lysine

Arginine

Titration

(isoelectric point)

pI= the pH at which the amino acid is electrically neutral, no charge.

The pI of a solution can be found by averaging the pKa1 and pKa2.

linear, partial double bond

read from N to C

breaks under high acid/temps

alpha helix: most common, spiral with 3.6 aa per turn, has keratin and proline/charged aa can disrupt

beta sheet: 2 peptide chains, pleated/parallel, antiparallel

beta bend: reverse direction on chain to make globe shape, protein surfaces, uses proline and glycine  

motifs

heart, skeletal muscle. oxgen carrier

single polyp chain that only carries 1 molecule

in RBCs, 2 alpha and 2 beta chinas, 4 oxygens, allosteric regulation (affinity increases with each oxygen)

T form (deoxy state)

R form (oxygen bound)

most abundarnt organic moleculein RBC. made from glycosidic pathway

decreases oxygen affinity of Hb.

ring structure that is bulky and kinky

in fibrous structures that interrupt globular alpha helixes.