amino acid structure and function Flashcards
what isomers are usually dealt with in biology
L isomers
hydrophobic amino acids
glycine alanine proline valine leucine isoleucine methionine tryptophan phenylalanine
polar amino acids
serine threonine tyrosine asparagine glutamine cysteine
which amino acids can participate in redox rxns?
cysteine
disulfide linkages
charged (+) amino acids
basic
lysine
arginine
histidine
charged (-) amino acids
acidic
aspartate (aspartic acid)
glutamate (glutamic acid)
small amino acids
alanine
glycine
cysteine
serine
proline
threonine
aspartic acid
asparagine
medium amino acids
valine
histidine
glutamic acid
glutamine
large amino acids
isoleucine leucine methionine lysine arginine
tyrosine
tryptophan
phenylalanine
essential amino acids
humans cannot synthesize; cannot make or cannot make enough
histidine lysine tryptophan isoleucine phenylalanine valine leucine threonine
consumption > production:
arginine
methionine
nonessential amino acids
humans can synthesize dev novo
alanine cysteine glycine asparagine glutamine proline aspartic acid glutamic acid serine
secondary synthesis:
tyrosine (can make it, but make it from a nonessential amino acid-phenylalanine
mnemonic for essential amino acids
Pvt Tim Hall (first letter of full name)
P henylalanine (Phe, F) V aline (Val, V) T ryptophan (Trp, W)
T hreonine (Thr, T) I soleucine (Ile, I) M ethionine (Met, M)
H istidine (His, H) A rginine (Arg, R) L ysine (Lys, K) L eucine (Leu, L)
proteinogenic amino acids
are used to make proteins from the genetic code
nonproteinogenic amino acids
are not decoded from the genome
e.x. post-translational modifications (phosphorylation for example)
21st amino acid
Selenocysteine (Sec, U)
pKa = 5.2
synthesized from serine
selenocysteine can be processed to:
selenomethionine in plants, algae, and yeast
and alanine in animals
stop codon for selenocysteine
UGA (opal)
selenocysteine is found in
all 3 domains of life (bacteria, archea, and eukaryea)