Protein levels
- Created by: Jasmin
- Created on: 19-10-13 18:16
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- Proteins - levels of structure
- Primary: sequence of AAs in the chain/protein, joined by peptide bonds
- Determines eventual shape
- Change in any of the AA will disturb bonding in 2, 3 levels
- Change in AA leads to change in shape of protein and may stop it from carrying out its function
- Determines eventual shape
- Secondary: the coiling or folding parts of a protein molecule due to formation of H bonds formed as protein is synthesised
- Coil into alpha helix or fold into beta pleated sheet
- H bonds form between the AAs in the chain
- Tertiary: overall 3D of shape. Result of interaction between parts of protein molecule such as H, disulphide, ionic bonding, interactions
- Coiled or folded chains coil or fold further
- Disulphide bonds
- Strong, not easily broken
- Less frequent than H bonds, more bonds form due to interactions between R groups of polypeptide chain
- Form between R groups containing sulphur bonds
- Ionic bonds
- Form between R groups with charges +ve and -ve
- Easily broken by changes in pH
- H bonds
- Weak, but numerous
- Lots of them together make a molecule hold its shape
- But individually easily broken down
- Hydrophobic: inside don't like water, Hydrophilic: outside, attracted to water
- Quaternary: Protein consists of more than one polypeptide chain. Haemoglobin/Insulin
- How chains are put together
- Haemoglobin- 4 polypeptide chains bonded together. Determines final structure
- Primary: sequence of AAs in the chain/protein, joined by peptide bonds
- Quaternary: Protein consists of more than one polypeptide chain. Haemoglobin/Insulin
- How chains are put together
- Haemoglobin- 4 polypeptide chains bonded together. Determines final structure
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