HUBS1403 Lecture Notes - Lecture 5: Nitrogenous Base, Cytosine, Hydrogen Bond

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Minimise changes in ph of cells and tissues. Enzymes accelerate chemical reactions: coordination and control. E. g lh, fsh (reproductive), growth hormone: defence: 20 different amino acids (aa) large 100000aa: 12 non-essential aa body can synthesise, 8 essential amino acids cant synethesis (we must consume) Every amino acid has: a central carbon atom, an amino group (base, a carboxyl group (-cooh) acidic, a side chain (r-group) different for each aa. Different properties depending on r group molecules. Non-polar: hydrophobic covalent bond between cooh group of 1aa and nh2 group of another forms of peptides i. e. - we make proteins by joining amino acids. Amino acids are linked by peptide bonds. Primary structure: the sequence of amino acids. Secondary structure due to bonds between nearby atoms in the chain (local folding) hydrogen bonding tertiary structure- complex coiling and folding final. 3d shape - primarily due to interactions b/n polypeptide and surrounding h2o - can involve r groups e. g. s-s.

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