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THE STRUCTURE AND FUNCTION OF MACROMOLECULES macromolecule: a "large" molecule that consists of small organic molecules classes: carbohydrates, lipids, proteins, nucleic acids examples: glucose, phospholipid, enzyme, DNA
most are built from polymers: chains of monomers (repeated units)
dehydration reaction: when monomers are linked together, a water molecule is removed (H from one monomer and OH from another) hydrolysis reaction: when polymers are disassembled a water is added (reverses the condensation reaction)
building a polymer with a limited list of monomers is like building words with a limited list of letters The differences in the arrangment of monomers into polymers is what makes organisms different. Its determined by the arrangement of nitrogen bases in a DNA molecule (recipe for life)
Carbohydrates monosaccharide simple sugar multiple units of CH2O range in number of carbons hexose, triose, pentose provides nutrients for cells, store energy for cells' use carbon skeletons can serve as raw material for other molecules examples: ribose, deoxyribose, glucose, dextrose, fructose, galactose disaccharide two simple sugars (monosaccharides) joined by glycosidic bonds assembled by dehydration reaction examples: maltose (glucose+glucose), sucrose (glucose+fructose), lactose (glucose+galactose) polysaccharide "complex carbohydrates" composed of many simple sugars (predominantly glucose) store energy or provide building material for other molecules examples: starch and glycogen (storage), cellulose and chitin (building material)
steroids carbon rings (4) hormones are created from cholesterol found in animal cell membranes (permeability and fluidity) saturated fats and trans fats change cholesterol levels in the blood
Proteins derived from a specific arrangement of polypeptides polymers created by 20 different amino acids folded and coiled into specific conformations primary unique sequence of amino acids secondary coils and folds resulting from hydrogen bonds between the backbone coil (alpha helix) folds (beta pleated sheet) tertiary overall shape resulting from interaction between the R groups (side chains) quaternary overall shape resulting from the aggregation of polypeptide subunits various types of proteins enzymatic proteins, structural proteins, storage proteins, transport proteins,hormonal proteins, receptor proteins, contractile and motor proteins, defensive proteins examples: digestive enzymes, collagen, casein, hemoglobin, insulin, membrane receptors, actin, antibodies amino acids carbon attached to a hydrogen, amino group, carboxyl group, and R group(side chain) linked together in a polypeptide by peptide bonds
metabolism: the sum of all chemical reactions of an organism metabolic pathways begin with a specific molecule, which is then altered in a series of defined steps, catalyzed by enzymes, resulting in a certain product
enzyme 1 enzyme 2 enzyme 3
-->
reaction 1
-->
reaction 2
-->
reaction 3
starting molecule
product
Catabolic pathways: the breakdown of complex molecules to smaller compounds releases energy example: cellular respiration hydrolysis also known as: breakdown pathways downhill Anabolic pathways: the building of complex molecules from smaller compounds consumes energy example: protein synthesis dehydration also known as: biosynthetic pathways uphill Energy released by the "downhill" reactions of catabolism can be stored and used to drive the "uphill" reactions of anabolism
Energy is defined as the capacity to cause change (rearrange a collection of matter)
biological catalysts: speed up chemical reactions by lowering the activation energy (EA) activation energy (EA): energy required to start a reaction often supplied in the form of heat
when enzymes lower the EA, they enable the reactants to absorb enough energy to reach the transition state.
"induced fit"
Optimal Conditions: 1. temperature: 35-40 degrees C (bacteria have enzymes that operate in greater temps (>70)) 2. pH: 6-8 (pepsin, stomach enzyme works best in pH of 2)
Enzymatic Inhibition inhibitors: molecules that bond to enzymes and reduce their function 1. competitive inhibition: inhibitor binds to active site 2. non-competitive inhibition: inhibitor binds to allosteric site changes conformation of enzyme
Cofactors and Coenzymes non-protein components that help enzymes function. help the active site bind to the substrate help the active site maintain its shape enzymatic function
Cofactors: inorganic molecules, such as ions or elements (copper, iron, zinc) Coenzymes: organic molecules, such as vitamins, which must come from diet