Protein structure
- Created by: Alice Fisher
- Created on: 06-05-15 20:00
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- Protein Structure
- Folding of a peptide into a protein
- Hydrophobic core region contains non-polar side chains. Polar side chains on outside can form hydrogen bonds with water. This can drive folding
- Held together by interactions; ionic (attraction between +ve and -ve), van der Walhs, electrical (attraction and repulsion), hydrogen bonds (involves O and N atoms forming a charge cloud)
- Primary structure read from left to right
- Secondary Structure
- a-helix, b-sheet, random coil
- 7 amino acids per 2 turns in an a-helix (heptaoid), intra-chain H bond runs vertically every 4th residue
- Interchain H bonds between b-sheets. Anti-parallel B-sheets have B-turns, parallel have long loops
- Random coil
- Everything between a-helix and b-sheet
- Tertiary Structure
- The way in which secondary structures pack together
- Src tyrosine kinase - a multidomain soluble protein (made of 4 functional domains)
- Quaternary Structure
- Relationship between individual proteins in a multimeric complex
- Post - translational modifications
- Disulphide bonds, proteolysis, glycosylsation, lipid modification, phosphorylation/ dephosophorylation
- Disulphide bonds typically found in proteins exposed to extremes of environment (conditions variable) e.g enzymes
- Proteolytic processing of precursor protein
- Active hormone or enzyme cleaved to yield a mature functional molecule
- Disulphide bonds, proteolysis, glycosylsation, lipid modification, phosphorylation/ dephosophorylation
- Folding of a peptide into a protein
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