W1 Proteins + Amino Acids Flashcards
what are prion proteins (PrP)
convert the normal form (PrPC) to the pathogenic form (PrPSc)
what does the polymerisation of PrPSc create
fibrils
what are amyloids
aggregates of misfolded proteins
what are optical isomers of AA known as
L and D isomers
what’s the diff between L and D isomers
D isomers cannot be digested
what type of ions do AA exist as
zwitterion ions
which isomer is most commonly found in proteins
L isomers
what are the 6 features of R groups
Size
Shape
Charge
Hydrogen bonding capacity
Hydrophobicity
Chemical reactivity
which AA has H as the R group
glycine
what do aliphatic R groups do to AAs
makes the amino acid more hydrophobic
what does the AA proline have
cyclic aliphatic r group
what are the 3 aromatic AA
Phenylalanine
Tyrosine
Tryptophan
what makes Serine and Threonine hydrophilic
OH groups
what are the 2 basic AA
Lysine and Arginine
which AA has a imidazole ring
histidine
where is histidine found mainly
active site of enzymes
what are the 2 acidic AA
Aspartic acid and Glutamic acid
how are Asparagine and Glutamine formed
NH2 group replaces O- group in COOH of Aspartate and Glutamate
what are the 7 AA with ionisable side chains
Aspartic acid (Asp, D)
Glutamic acid (Glu, E)
Histidine (His, H)
Lysine (Lys, K)
Arginine (Arg, R)
Cysteine (Cys, C)
Tyrosine (Tyr, Y)
how heavy is 1 Dalton (DA)
1 hydrogen atom
how are mass of proteins quoted
in kDA
how far is 1 Angstrom (Å)
0.1 nm
what is the distance between CO and NH groups
1.32Å
how are peptide bonds described as shape wise
planar
