03 proteins

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Information about 03 proteins

Published on March 15, 2014

Author: nutran9

Source: slideshare.net



PRIMARY STRUCTURE  The numbers of amino acids vary (e.g. insulin 51, lysozyme 129, haemoglobin 574, gamma globulin 1250)  The primary structure determines the folding of the polypeptide to give a functional protein  Polar amino acids (acidic, basic and neutral) are hydrophilic and tend to be placed on the outside of the protein.  Non-polar (hydrophobic) amino acids tend to be placed on the inside of the protein © 2007 Paul Billiet ODWS

Infinite variety  The number of possible sequences is infinite An average protein has 300 amino acids, At each position there could be one of 20 different amino acids = 10390 possible combinations  Most are useless Natural selection picks out the best © 2007 Paul Billiet ODWS

SECONDARY STRUCTURE The folding of the N-C- C backbone of the polypeptide chain using weak hydrogen bonds © Science Student © Text 2007 Paul Billiet ODWS

SECONDARY STRUCTURE  This produces the alpha helix and beta pleating  The length of the helix or pleat is determined by certain amino acids that will not participate in these structures (e.g. proline) © Dr Gary Kaiser © Text2007 Paul Billiet ODWS

TERTIARY STRUCTURE The folding of the polypeptide into domains whose chemical properties are determined by the amino acids in the chain MIL1 protein © Anne-Marie Ternes © 2007 Paul Billiet ODWS

TERTIARY STRUCTURE  This folding is sometimes held together by strong covalent bonds (e.g. cysteine-cysteine disulphide bridge)  Bending of the chain takes place at certain amino acids (e.g. proline)  Hydrophobic amino acids tend to arrange themselves inside the molecule  Hydrophilic amino acids arrange themselves on the outside © 2007 Paul Billiet ODWS

© Max Planck Institute for Molecular Genetics Chain B of Protein Kinase C

QUATERNARY STRUCTURE Some proteins are made of several polypeptide subunits (e.g. haemoglobin has four) Protein Kinase C © Max Planck Institute for Molecular Genetics © Text 2007 Paul Billiet ODWS

QUATERNARY STRUCTURE  These subunits fit together to form the functional protein  Therefore, the sequence of the amino acids in the primary structure will influence the protein's structure at two, three or more levels © 2007 Paul Billiet ODWS

Result Protein structure depends upon the amino acid sequence This, in turn, depends upon the sequence of bases in the gene © 2007 Paul Billiet ODWS

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 © 2007 Paul Billiet ODWS

Fibrous proteins  Involved in structure: tendons ligaments blood clots (e.g. collagen and keratin)  Contractile proteins in movement: muscle, microtubules (cytoskelton, mitotic spindle, cilia, flagella) © 2007 Paul Billiet ODWS

Globular proteins  most proteins which move around (e.g. albumen, casein in milk)  Proteins with binding sites: enzymes, haemoglobin, immunoglobulins, membrane receptor sites © 2007 Paul Billiet ODWS

Proteins classified by function  CATALYTIC: enzymes  STORAGE: ovalbumen (in eggs), casein (in milk), zein (in maize)  TRANSPORT: haemoglobin  COMMUNICATION: hormones (eg insulin) and neurotransmitters  CONTRACTILE: actin, myosin, dynein (in microtubules)  PROTECTIVE: Immunoglobulin, fibrinogen, blood clotting factors  TOXINS: snake venom  STRUCTURAL: cell membrane proteins, keratin (hair), collagen © 2007 Paul Billiet ODWS

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