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Summary OCR A/AS-Level Biology 2.2.9-10 Proteins £2.99   Add to cart

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Summary OCR A/AS-Level Biology 2.2.9-10 Proteins

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Revision summary of key knowledge from OCR A/AS-Level Biology 2.2.9-10 Proteins.

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  • Chapter 2.2.9-10
  • June 26, 2023
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  • 2022/2023
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Protein Structure
Peptide Bonds
 Covalent bonds formed by condensation reactions between amino and carboxyl groups
 All amino acids join in the same way, regardless of the R group
 Two amino acids joined together is known as a dipeptide
 More amino acids joined in a chain are known as a polypeptide




Levels of Protein Structure
 Primary structure – the sequence (number and order) of amino acids
 Secondary structure – the coiling or folding of an amino acid chain resulting from
hydrogen bonds between different parts of the chain – main forms are an alpha helix or
beta pleated sheet
 Tertiary structure – overall 3D shape of a protein molecule
 Quaternary structure – protein structure when a protein consists of multiple
polypeptide chains

Other Protein Bonds
 Hydrogen bonds – form between hydrogen atoms with a slight positive charge (δ+) and
other atoms with a slight negative charge (δ-) – found in hydroxyl, carboxyl and amino
groups
 Ionic bonds – form in R groups where eth amino and carboxyl groups ionise – these are
very strong bonds
 Disulfide bridges – string covalent bonds between R groups containing sulfur
 Hydrophobic interactions – hydrophobic parts of the R group associate together in the
centre of the polypeptide, away from water
 Hydrophilic interactions – hydrophilic parts of the R group are found around the edge of
the polypeptide, close to water

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