Published on March 15, 2014
PROTEINS FOLDED POLYPEPTIDES © 2007 Paul Billiet ODWS
PRIMARY STRUCTURE The sequence of amino acids MIL1 sequence: >gi|7662506|ref|NP_056182.1| MIL1 protein [Homo sapiens] MEDCLAHLGEKVSQELKEPLHKALQMLLSQPVTYQAFRECTLETTVHASGWNKILVPLVLLRQMLL ELTRLGQEPLSALLQFGVTYLEDYSAEYIIQQGGWGTVFSLESEEEEYPGITAEDSNDIYILPSDN SGQVSPPESPTVTTSWQSESLPVSLSASQSWHTESLPVSLGPESWQQIAMDPEEVKSLDSNGAGEK SENNSSNSDIVHVEKEEVPEGMEEAAVASVVLPARELQEALPEAPAPLLPHITATSLLGTREPDTE VITVEKSSPATSLFVELDEEEVKAATTEPTEVEEVVPALEPTETLLSEKEINAREESLVEELSPAS EKKPVPPSEGKSRLSPAGEMKPMPLSEGKSILLFGGAAAVAILAVAIGVALALRKK length: 386amino acids © Anne-Marie Ternes
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
Ivetic, A., Ridley, A.J. (2004): Ezrin/radixin/moesin proteins and Rho GTPase signalling in leukocytes. Immunology. 112, 165–176; Machesky, L.M., ...
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03 Proteins - Download as Powerpoint Presentation (.ppt), PDF File (.pdf), Text File (.txt) or view presentation slides online.
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Protein structure is the three-dimensional arrangement of atoms in a protein molecule. Proteins are polymers — specifically polypeptides — formed from ...
PROTEINS. FOLDED POLYPEPTIDES © 2007 Paul Billiet ODWS PRIMARY STRUCTURE The sequence of amino acids MIL1 sequence: >gi|7662506|ref|NP_056182.1 ...
Protein. 1. Amino Acids. Amino acids are hydrophobic, hydrophilic, or have special properties; Amino acids consist exclusively of the L-isomer. Proline is ...
Proteins are assembled from amino acids using information encoded in genes. Each protein has its own unique amino acid sequence that is specified by the ...
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