Large proteins consist of more than one polypeptide chain and possibly a non-peptide prosthetic group.The polypeptide chains are held together by ionic, covalent (disulfide bridges) and hydrogen bonds.Hydrophobic interactions are attractive forces between non-polar groups in aqueous environments.Hydrophilic interactions are attractive forces between polar groups in aqueous environments and water molecules.Both hydrophobic and hydrophilic interactions affect the tertiary and quaternary structure of proteins.
Quaternary Structure
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Specification: AQA Biology (7401), AS-level, 3.1.4.1 General properties of proteins. Topic: Biological Molecules.
Key terms in this lesson
- hydrogen bond
- A weak electrostatic attraction between a slightly positive hydrogen atom on one polar molecule and a slightly negative atom, such as oxygen or nitrogen, on another.
- disulfide bridge
- A strong covalent bond formed between two sulfhydryl (-SH) groups of cysteine residues in a polypeptide.
More in Biological Molecules
- Amino-Acids
- Peptide Bond Formation
- Primary Structure
- Secondary Structure
- Tertiary Structure
- Test for Proteins
- Globular and Fibrous Proteins
- Collagen
All 29 lessons in Biological Molecules · All AQA AS-level Biology topics