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post translational modification
alter the properties of the amino acid, which can alter the structure and function of the protein
phosphorylation
serine, threonine, tyrosine
hydroxylation
proline, lysine
acetylation
lysine, serine, threonine
methylation
lysine, glutamate
carboxylation
glutamate
AMP-ylation
threonine, tyrosine
N/O-glycosylation
asparagine, serine, threonine
disulfide bond formation
cysteine
ubiquitylation
lysine
SUMO-ylation
lysine
deamidation
asparagine, glutamine
histone acetylation
acetylases transfer acetyl groups from acetyl-CoA to lysine residues on histones
weakens the interaction between histones and DNA, leading to a less condensed and more accessible chromatin structure
deacetylases remove acetyl groups from lysine residues and cause chromatin to compact
erythropoietin glycosylation
blood-stimulating hormone erythropoietin has N- and O-linked oligosaccharides contributing to its function and stability
ubiquitylation process
addition of a small protein called [name] on to other proteins: helps with protein degradation
proteolysis process
proteases enzymatically hydrolyze peptide bonds in substrate proteins