2.4. Protein Structure Flashcards
Primary structure
Sequence of amino acids as determined by mRNA codons
- contains peptide bonds
Secondary structure
- Two regular folding patterns (alpha helix and beta pleated sheet) are formed as dictated by amino acids in primary sequence (secondary structure)
- results from hydrogen-bonding between between N-H & C=O groups in the polypeptide backbone
Alpha helix (secondary structure)
- Single polypeptide chain twists to form a rigid cylinder
2. Hydrogen bonds within polypeptide chain spaced 4 amino acids apart
Beta pleated sheet (secondary structure)
- Rigid planar structures with hydrogen bonds between amino acids in adjacent strands
- Can form from parallel chains or anti parallel chains
Parallel chains
Neighboring polypeptide chains that run in the same orientation
Antiparallel chain
- Polypeptide chain that folds back and forth upon itself, with each section of the chain running in the direction opposite to that of its immediate neighbours
Tertiary structure
3D structure of polypeptide chain
- Disulphide bonds
- Hydrogen bonds
- Ionic bonds
- Hydrophobic interactions
- van der waals forces
- formed by secondary structures folding with each other
- highest level of organization in monomeric proteins
Quaternary structure
- describes the number and relative positions of subunits in multimeric proteins
Dynamic
Modify proteins & elicit changes in cellular function
PTM
Post translational modifications
Proportion
Form protein translated as before being activated by removal of amino terminal amino acids
Phosphorylation
- Addition of a phosphate molecule
Protein kinases
Enzymes that facilitate transfer of phosphate
Phosphorylases
Help to remove phosphate
Methylation
Addition of methyl (CH3)