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Terms in this set (16)
What levels of organisation apply to all protein?
Primary, secondary and tertiary structures.
What are the permanent non-amino acid components of proteins?
Cofactor and prosthetic groups. Prosthetic groups are the best answer as cofactors are reversible.
Non covalent interactions in protein structure
Hydrophobic, electrostatic, hydrogen bonds, VDW
Identify the modification that creates elasticity
Desmosine - ring structure can be stretched in all directions
Products formed by the action of kinases
Kinases add a phosphate group. Phosphoserine, phosphotyrosine and phosphothreonine. Phosphotases do the opposite.
The modification of proline to hydroxyproline often includes a vitamin, which is...?
Vitamin C (ascorbic acid). acts as a cofactor, which required for proper functioning of collagen - leads to scurvy.
Peptide bond formation
Condensation and hydrolysis
What should be avoided in PKU disease?
Maple syrup disease suffers should avoid..
Leucine, isoleucine and valine
Alpha helix characteristics
3.6 residues a turn
Hydrogen bonding stabilises
R groups on outside
Disrupter of alpha helix
proline as cis and trans form create destabilising kink
Modification not found in humans
Pyrolysine. 22 Amino acid. Found in archeabacteria
Two SH from two cysteines are oxidised. Hydrogens are removed and the disulphide bond is formed. This is characterised by two sulphers, which forms one cystine.
EDS, collagen imperfecta
- Made up of beta sheets layered on top of each other
- Large concentration of alanine and lysine
- Different types of silk - stronger, elastic ect
- Has small side chains
Glutamate - gammacarboxyglutamate conversion, will there be a charge?
Glutamate: one of the two acidic amino acids, this means it has a carboxylate side chain
Gamme: has a second carboxy added to it, this adds a second negative charge
So there are 2 negative charges
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