Proteins

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Last updated 4:26 PM on 7/13/26
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21 Terms

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amino acid

monomers that link together to form polypeptides and proteins, they contain an amino group (NH2), a carboxyl group (COOH), a hydrogen atom, and a variable R group

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dipeptide

a molecule of 2 amino acids joined together by a peptide bond

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polypeptide

a chain of amino acids joined by peptide bonds

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R - group

variable part of amino acid that differs one amino acid to another

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Amine group

functional group for all amino acids, (NH2)

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peptide bond

a covalent bond between the carboxyl group of one amino acid and the amino group of another

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hydrogen bonds

hydrogen bond forms between hydrogen atom and an oxygen or nitrogen atom, helping to maintain the shape of proteins and DNA

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ionic bonds

formed by attraction between oppositely charged ions. In proteins, ionic bonds form between positively and negatively charged R groups

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disulfide bridge

strong covalent bond between two cysteine amino acids, helping to stabilise a proteins 3D structure

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cysteine

amino acid that contains a sulfur containing R group

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alpha helix

arrangement of polypeptide chain stabilised by hydrogen bonds between the peptide backbone

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beta pleated sheet

formed by folded polypetide chains, important in secondary structure of proteins

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enzyme

a biological catalyst which speeds up a chemical reaction without being used up

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antibodies

proteins produced by the immune system that recognise and bind to specific antigen and helps the body to defend against infection

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Transport proteins

proteins that carry specific molecules or ions across a membrane

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structural proteins

protein that forms physical structures and helps maintain the shape and strength of tissues

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biuret test

chemical test to detect proteins, solution changes from blue to lilac

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Primary structure

specific sequence of amino acids in a polypeptide chain.

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Secondary structure

secondary structure of a protein is the local folding of the polypeptide chain into an alpha helix or beta pleated sheet, stabilised by hydrogen bonds between the peptide backbone.

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Tertiary structure

the three-dimensional shape formed when a polypeptide folds due to interactions between the R groups of its amino acids.

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Quaternary structure

quaternary structure of a protein is formed when two or more polypeptide chains associate and are held together to make a functional protein.