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The Structure and Function of Large Biological Molecules (Lipids-compounds…

- - - - Dehydrating reaction-a reaction in which two molecules are covalently bonded to each other with the loss of a molecule
        
        Hydrolysis-a process that essentially is the reverse of the dehydration reaction
      - Polysaccharides-polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages
        
        starch-plant polysaccharides that work as stored energy and used when needed through hydrolysis
        
        glycogen- a polymer of glucose used by animals to supply sugar when needed
        
        Polymer-a long molecule consisting of many similar or identical monomers linked together by covalent bonds
        
        cellulose-major component of the tough walls that enclose plant cells
        
        chitin-a polysaccharide that creates the exoskeleton of arthropods(insects)
- - - - in making a fat, three fatty acid molecules are each joined to glycerol by an ester linkage. a bond formed by a dehydration reaction between hydroxyl group and carboxyl group
        
        This results in the creation of triacylglycerol, thus consists of three fatty acids linked to one glycerol molecule.
      - Saturated fatty acid-a fatty acid in which all carbons in the hydrocarbons tail are connected by single bonds, thus maximizing the number of hydrogen atoms that are attached to the carbon skeleton. more hydrogen atoms=saturated by hydrogen bonds. Hydrogen bonds because of the lack of double bonds between carbon atoms attracting hydrogen atoms.
      - Unsaturated fatty acid- a fatty acid that has one or more double bonds between carbons in the hydrocarbon tail. Such bonding reduces the number of hydrogen atoms attached to the carbon skeleton. Contains double bonds preventing excess hydrogen.
        
        Trans fat-an unsaturated fat, formed artificially during the hydrogenation of oils, containing one or more trans double bond
- - - - Protein-a biologically functional molecule made up of one or more polypeptides
        
        Enzymatic proteins: Function selective acceleration of chemical reactions. Example- digestive enzyme, catalyse the hydrolysis bonds in food
        
        Storage proteins-stores amino acid Example: Casein-The protein of milk, is the major source of amino acids for baby mammals.
        
        Hormonal Proteins-coordination of an organisms activities. Example: Insulin, a hormone from the pancreas, causes other tissues to take up glucose, thus regulating blood sugar concentration.
        
        Contractile and motor proteins-movement Example: Motor proteins are responsible for the undulation(wave like movement) of cilia and flagella which produce movement of the body.
        
        Defensive proteins-Protection of disease. Example- antibodies inactivate and help destroy viruses and bacteria
        
        Transport proteins-Transport of substances. Example- hemoglobin -the iron containing protein of vertebrate blood, transports oxygen from the lungs to the rest of my body
        
        Receptor Proteins-Response of cell to chemical stimuli. Example-Receptors built into the membrane of a nerve cell detect signaling molecules released by other nerve cells.
        
        Structural proteins-support. Example-Keratin is the protein in hair horns or feather that lend strength to its overall structure
        
        What is a side chain R groups?
        
        Primary structure- of a protein is its sequence of amino acids.
        
        Secondary Structure- proteins with segments of their polypeptide chains repeatedly coiled or folded in patterns that contribute to the overall shape of the protein. Caused by its hydrogen bond between the molecules that make up
        
        Tertiary structure- overall shape of a polypeptide when viewing the interractions between the side chains (R groups) of amino acids.
        
        hydrophobic= nonpolar
        
        Hydrophobic Interaction-when amino acids that are nonpolar meet in the center of the protein
        
        Disulfide Bridges-covalent bonds that reinforce the shape of a protein. when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer
        
        Quaternary Structure- protein consisting of two or more polypeptide chains aggregated into one functional macromolecule
        
        Sickle Cell disease-a inherited blood disorder caused by the substitution of one amino acid (valine) for the normal one (glutamic acid) at the position of the sixth amino acid in the primary structure of hemoglobin, the protein that carries oxygen through the body in red blood cells
        
        Denaturation- When chemical bonds breakup because conditions are not ideal for it. Or they remain inactive.
        
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- - - - Macromolecules that exist as polymers called polynucleotides
        
        Polynucelotides consist of monomers called nucleotides, which is composed of three parts:
        
        A five carbon sugar
        
        Attached to nitrogenous bases- known as deoxyribose in DNA the Difference is the lack of an oxygen atom on the second carbon ring.
        
        In RNA it is ribose
        
        a nitrogen base
        
        One or two rings that include nitrogen atoms
        
        Pyrimidine-one of the two types of nitrogen bases. Contains one six membered ring of carbon and nitrogen atoms.
        
        The members of this family are cytosine(C). Thymine(T), and Uracil(U),
        
        Purines-Larger six membered ring fused to a five-membered ring.
        
        Adenine (A) and Guanine(G)
        
        one to three phosphate groups
        
        The beginning monomer used to build a polynucleotide has three phosphate groups but two are lost during its fusion process
        
        All three lead to a Nucleotide polymer caused by nucleotides having a dehydration reaction creating a polynucleotide.
        
        In the DNA, Double helix contains bases that connect with one another.
        
        The outside of the double helix the lines are referred to as the sugar phosphate backbone
        
        The inside strands are known as nitrogenous bases are held together by hydrogen bonds between the paired bases
        
        Only certain bases combine: Adenine with Thymine, Guanine and Cytosine
        
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        Genomics-looking at problems by analyzing large sets of genes or even comparing whole genomes of different species
        
        Proteomics- a similar analysis of large sets of protein.
  - - - This process is known as gene expression
        
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        DNA->RNA->Protein