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Edit Comment Close Premium member Presentation Transcript Protein Structure : Protein Structure Protein Structure Different Amino Acid Classes : Different Amino Acid Classes Protein Structure Non-PolarAmino Acids : Non-PolarAmino Acids Protein Structure Polar Amino Acids : Polar Amino Acids Protein Structure Acidic Amino Acids : Acidic Amino Acids Protein Structure Basic Amino Acids : Basic Amino Acids Protein Structure Levels Of Protein Organization : Levels Of Protein Organization Primary Structure - The sequence of amino acids in the polypeptide chain Secondary Structure - The formation of a helices and b pleated sheets due to hydrogen bonding between the peptide backbone Tertiary Structure - Folding of helices and sheets influenced by R group bonding Quaternary Structure - The association of more than one polypeptide into a protein complex influenced by R group bonding Protein Structure Levels Of Protein OrganizationPrimary Structure : Levels Of Protein OrganizationPrimary Structure Met-Gly-Ala-Pro-His-Ile-Asp-Glu-Met-Ser-Thr-... The sequence of amino acids in the primary structure determines the folding of the molecule. Protein Structure Protein Secondary Structure : Protein Secondary Structure The peptide backbone has areas of positive charge and negative charge These areas can interact with one another to form hydrogen bonds The result of these hydrogen bonds are two types of structures: a helices b pleated sheets Protein Structure Protein Secondary Structure:a Helix : Protein Secondary Structure:a Helix Protein Structure Protein Secondary Structure:a Helix : Protein Secondary Structure:a Helix Protein Structure Protein Secondary Structure:a Helix : Protein Secondary Structure:a Helix R groups stick out from the a helix influencing higher levels of protein organization Protein Structure Yeast Cytochrome C Oxidase Subunit IV Leader : Yeast Cytochrome C Oxidase Subunit IV Leader MLSLRQSIRFFKPATRTLCSSRYLL This would localise specific classes of amino acids in specific parts of the helix Neutral Non-polar Polar Basic Acidic Protein Structure Protein Secondary Structure:b Pleated Sheet : Protein Secondary Structure:b Pleated Sheet Protein Structure Protein Secondary Structure:b Pleated Sheet : Protein Secondary Structure:b Pleated Sheet Protein Structure Levels Of Protein OrganizationTertiary Structure : Levels Of Protein OrganizationTertiary Structure Tertiary structure results from the folding of a helices and b pleated sheets Factors influencing tertiary structure include: Hydrophobic interactions Hydrogen bonding Disulphide bridges Ionic bonds Protein Structure Hydrophobic interactions : Hydrophobic interactions Protein Structure Hydrogen Bonding : Hydrogen Bonding N-------H (+) (-) O -------C slightly slightly Protein Structure Disulphide bridges : Disulphide bridges Protein Structure Ionic Bonds : Ionic Bonds Protein Structure e.g.G-3-P DehydrogenaseTertiary Structure : e.g.G-3-P DehydrogenaseTertiary Structure Picture source: SWISS-PROT Protein Structure Levels Of Protein OrganizationQuaternary Structure : Levels Of Protein OrganizationQuaternary Structure Quaternary structure results from the interaction of independent polypeptide chains Factors influencing quaternary structure include: Hydrophobic interactions Hydrogen bonding The shape and charge distribution on amino acids of associating polypeptides Protein Structure G-3-P Dehydrogenasefrom Bacillus stearothermophilus : G-3-P Dehydrogenasefrom Bacillus stearothermophilus Picture source: SWISS-PROT Protein Structure Globular and Fibrous : Globular and Fibrous e.g. haemoglobin 3º structure normally folds up in a ball hydrophilic R groups point outwards Hydrophobic R groups point inwards soluble metabolic functions e.g. collagen 2º structure does not fold up, form fibres not surrounded by hydrophilic R groups insoluble structural functions Protein Structure Haemoglobin : Haemoglobin Haemoglobin is a globular protein with a prosthetic ‘iron’ group In adults, hemoglobin is made up of 4 polypeptides (2 a polypeptide chains and 2 b polypeptide chains) Each polypeptide surrounds a prosthetic ‘haem’ group Hydrophobic interactions between side groups pointing inwards maintain the structure Hydrophilic side chains point outwards making it soluble Protein Structure Primary structure determines function : Primary structure determines function In the primary structure of the b polypeptide chains a mutation can cause a change in one of the amino acids. A polar glutamic acid is changed to a non-polar valine When the protein folds up the non-polar valine is pointing outwards and the haemoglobin is less ____________? Protein Structure Sickle Cell Anaemia : Sickle Cell Anaemia Protein Structure Haemoglobin : Haemoglobin Picture source: SWISS-PROT Protein Structure Slide 29: Collagen is a fibrous protein made of 3 polypeptide helices held together by hydrogen bonding Every 3rd amino acid in the chain is a glycine (very small to let the chains lie close to each other) Collagen molecules are found side by side forming fbres The staggered ends help to give collagen fibres great tensile strength Protein Structure Collagen and Vitamin C : Collagen and Vitamin C Vitamin C helps the conversion of the amino acid proline to hydroxyproline Hydroxyproline makes more hydrogen bonds and the collagen is stronger Protein Structure Scurvey : Scurvey Protein Structure You do not have the permission to view this presentation. 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