MCBM Exam 1 Save
Terms in this set (849)
aspartic acid Asp, D negative side chain
glutamic acid Glu, E negative side chain
arginine Arg, R positive side chain
lysine Lys, K positive side chain
histidine His, H positive side chain
asparagine Asn, N polar side chain
Glutamine Gln, Q polar side chain
serine Ser, S polar side chain
threonine Thr, T polar side chain
tyrosine Tyr, Y polar side chain
alanine Ala, A nonpolar
glycine Gly, G nonpolar
valine Val, V nonpolar
leucine Leu, L nonpolar
isoleucine Ile, I nonpolar
proline Pro, P nonpolar
phenylalanine Phe, F nonpolar
methionine Met, M nonpolar
Tryptophan Trp, W nonpolar
cysteine Cys, C polar
peptide bond formed by condensation rxn
, proteins are written with left
the N-terminus to the
alpha carbon of protein rigid
is rigid or flexible?
>50 amino acids polypeptides
<50 amino acids peptides
insulin is a polypeptide
oxytocin is a peptide
sex-peptide is a peptide think fruit fly mating
1. the amino acid sequence (primary structure)
native protein structure is
2. the physical and chemical properties of the side
determined by
chains
tendency of non polar groups to cluster so as to
hydrophobic effect shield themselves from contact with an aqueous
environment
most energetically avoid contact btwn water and hydrophobic groups
favorable step of folding
process is to
a linear protein has
clusters of hydrophobic
amino acid and clusters
of polar amino acids
amino acids whose serine, threonine, tyrosine
hydroxyl groups can
form a hydrogen bond
amino acids whose asparagine and glutamine
carbonyl and amine
groups can form
hydrogen bonds
amino acid whose side cysteine
chain can form disulfide
bond
Terms in this set (849)
aspartic acid Asp, D negative side chain
glutamic acid Glu, E negative side chain
arginine Arg, R positive side chain
lysine Lys, K positive side chain
histidine His, H positive side chain
asparagine Asn, N polar side chain
Glutamine Gln, Q polar side chain
serine Ser, S polar side chain
threonine Thr, T polar side chain
tyrosine Tyr, Y polar side chain
alanine Ala, A nonpolar
glycine Gly, G nonpolar
valine Val, V nonpolar
leucine Leu, L nonpolar
isoleucine Ile, I nonpolar
proline Pro, P nonpolar
phenylalanine Phe, F nonpolar
methionine Met, M nonpolar
Tryptophan Trp, W nonpolar
cysteine Cys, C polar
peptide bond formed by condensation rxn
, proteins are written with left
the N-terminus to the
alpha carbon of protein rigid
is rigid or flexible?
>50 amino acids polypeptides
<50 amino acids peptides
insulin is a polypeptide
oxytocin is a peptide
sex-peptide is a peptide think fruit fly mating
1. the amino acid sequence (primary structure)
native protein structure is
2. the physical and chemical properties of the side
determined by
chains
tendency of non polar groups to cluster so as to
hydrophobic effect shield themselves from contact with an aqueous
environment
most energetically avoid contact btwn water and hydrophobic groups
favorable step of folding
process is to
a linear protein has
clusters of hydrophobic
amino acid and clusters
of polar amino acids
amino acids whose serine, threonine, tyrosine
hydroxyl groups can
form a hydrogen bond
amino acids whose asparagine and glutamine
carbonyl and amine
groups can form
hydrogen bonds
amino acid whose side cysteine
chain can form disulfide
bond
