AMINO ACIDS & PROTEINS C, H, O, N, S © 2016 Paul Billiet ODWS.

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Presentation transcript:

AMINO ACIDS & PROTEINS C, H, O, N, S © 2016 Paul Billiet ODWS

Amino acids amino group, carboxyl group, hydrogen and a variable side group (residue) each joined to a central carbon atom H2N-C-COOH R H © 2016 Paul Billiet ODWS

Types of amino acids Amino end and carboxyl end can be ionised NH3+ and COO- to give acidic and basic characteristics At pH 7 both groups are ionised The residues are side chains which give the individual properties to the amino acid (acidic, basic, neutral and nonpolar). © 2016 Paul Billiet ODWS

Functions of amino acids Protein synthesis, energy reserves, hormones (thyroxin) 20 different amino acids used in protein synthesis though others do occur in nature Essential amino acids cannot be synthesised by the organism and must form part of their diet. © 2016 Paul Billiet ODWS

The peptide bond Carboxyl group + amino group form a strong covalent bond releasing water in the process = a condensation reaction (the reverse is hydrolysis) Amino acids join together in a long chain: N terminal end to C terminal end = a polypeptide. © 2016 Paul Billiet ODWS

Condensation reaction A dipeptide is formed N C C-OH R H O Condensation reaction A dipeptide is formed N C C R H O N C C-OH + H2O The peptide bond © 2016 Paul Billiet ODWS

Protein structure Primary structure MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE The primary structure of human cytochrome C Each letter represents an amino acid This protein has 105 amino acids. © 2016 Paul Billiet ODWS

Protein structure 3-D structure of human cytochrome C

PROTEIN FUNCTIONS Protein structure determines protein function Denaturation or inhibition which may change protein structure will change its function Coenzymes and cofactors in general may enhance the protein's structure. © 2016 Paul Billiet ODWS

Fibrous proteins Involved in structure: tendons ligaments blood clots (e.g. collagen and spiders silk) Contractile proteins in movement: muscle, microtubules (cytoskelton, mitotic spindle, cilia, flagella). © 2016 Paul Billiet ODWS

Globular proteins most proteins which move around (e.g. albumen, casein in milk) Proteins with binding sites: enzymes, hemoglobin, immunoglobulins, membrane receptor sites. © 2016 Paul Billiet ODWS

Proteins classified by function CATALYTIC: enzymes eg rubisco COMMUNICATION: hormones (eg insulin) and neurotransmitters PROTECTIVE: eg immunoglobulin, fibrinogen, blood clotting factors STRUCTURAL: eg collagen, spiders silk PIGMENTS: eg rhodopsin STORAGE: eg ovalbumen (in eggs), casein (in milk) TRANSPORT: eg hemoglobin CONTRACTILE: eg actin, myosin TOXINS: eg snake venom © 2016 Paul Billiet ODWS