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alanine
nonpolar side chain
hydrophobic
no H-bond
valine
nonpolar side chain
hydrophobic
no H-bond
leucine
nonpolar side chain
hydrophobic
no H-bond
isoleucine
nonpolar side chain
hydrophobic
no H-bond
methionine
nonpolar side chain
hydrophobic
no H-bond
phenylalanine
nonpolar side chain
hydrophobic
no H-bond
tryptophan
nonpolar side chain
hydrophobic
no H-bond
aspartate
polar: negatively charged
typically deprotonated at physiological pH
glutamate
polar: negatively charged
typically deprotonated at physiological pH
lysine
polar: positively charged
pKa 10.5
protonated and positively charged at physiological pH
arginine
polar: positively charged
pKa 12.5
protonated and positively charged at physiological pH
histidine
polar: positively charged
pKa 6.0
partially protonated at physiological pH
serine
polar: uncharged
hydrophilic
not typically ionized at physiological pH
threonine
polar: uncharged
hydrophilic
not typically ionized at physiological pH
glutamine
polar: uncharged
hydrophilic
not typically ionized at physiological pH
asparagine
polar: uncharged
hydrophilic
not typically ionized at physiological pH
tyrosine
polar: uncharged
hydrophilic
not typically ionized at physiological pH
glycine
only H atom as side chain
not chiral
can reside in sites where two polypeptides come into close contact
cysteine
polar, uncharged
can form covalent bond to make a disulfide link
proline
hydrophobic character
can create kinks in polypeptide chains and disrupt secondary structure