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Bonds In
Proteins
- Hydrogen bonds
- Groups with a slight negative charge will be
attracted to those with a slight positive charge
- Hydrogen bonds are quite weak, but can be easily broken by
changes in the temperature and pH
- Hydrogen bonds are quite weak, but can be easily broken by
changes in the temperature and pH
- Groups with a slight negative charge will be
attracted to those with a slight positive charge
- Disulphide bonds
- Disulphide bonds are strong covalent bongs(where electrons are shared between
atoms) formed between two cysteine amino acids
- Disulphide bonds are very strong, but can be
broken by reducing agents
- Disulphide bonds are very strong, but can be
broken by reducing agents
- Disulphide bonds are strong covalent bongs(where electrons are shared between
atoms) formed between two cysteine amino acids
- Ionic bonds
- Ionic bonds form between molecules that have a full positive or negative charge
- Ionic bonds are very strong, but can be broken by changes in pH
- Ionic bonds are very strong, but can be broken by changes in pH
- Ionic bonds form between molecules that have a full positive or negative charge
- Hydrophobic interactions
- R-groups that only contain hydrogen or carbon atoms are
hydrophobic, and are slightly attracted to each other
- These interactions are very weak and are easily broken
- These interactions are very weak and are easily broken
- R-groups that only contain hydrogen or carbon atoms are
hydrophobic, and are slightly attracted to each other
- The 3D shape of a protein is maintained by several types of bond including:
hydrogen bonds-involved in all levels of structure,hydrophobic interactions-between
non-polar sections of the protein and disulfide bonds- one of the most important
type of bond in proteins. occur between two cysteine amino acids.
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