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Fibrous proteins
insoluble and provide structure
cytoskeleton
coatings (seeds)
ie silk
Globular
enzymes (catalysts)
transport protein (haemoglobin)
hormones (insulin)
defense (antibodies)
toxins (snake venom)
Receptor (rhodopsin)
Amino acid: general structure

Zwitterionic
posesses both positive and negative charges
Chiral
amino acid property- only L amino acids exist in biology (glycine is not chiral)
Amino acid properties
Zwitterionic
Chiral
range of sidechain / R groups
Aliphatic
No charge on sidechain
increasing in hydrophobicity with sidechain size
Glycine, Alanine, Valine, Leucine, Isoleucine
Imino acid
only amino acid with a secondary amine group present. all others primary amines
sidechain from 5 membered ring- looping from the c alpha to the nitrogen
confers diff properties on the polypeptide chain
proline
Polar
sidechains contains hydroxyl groups
H-bond acceptors/ donors
hydrophbic in nature
Serine, Threonine
Basic
Lysine, Arginine, Histidine
Which amino acid has a pKa of 10
lysine
which amino acid has a pKa of 12
Arginine
which amino acid has a pKa of 6.5
Histidine
Acidic and amide derivatives
change o- (carboxyl group) to H2N
Aspartate, Aspargenine, Glutamate, Glutamine
Formation of a peptide bond:
Carboxylic acid reacts with amine
how do you estimate molecular mass of a protein
take number of amino acids and multiply by 110
how do you describe an amino acid
start at N- terminus (Amide) and then end at C terminus (hydroxyl group)