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BIO 120 Chapter 5

Large Biological Molecules

Polymer- made up of many parts
Monomer- made up of one part
Dehydration Reaction- requires energy and enzymes to remove water molecule, building a polymer
Hydration Reaction- Adds water molecule to break bond, break apart polymers
Carbohydrates- sugars and polymers of sugar, made up of carbon backbone
Monosaccharides- simplest form of a CH2O chain, 3-7 carbons long
Polysaccharide- carbohydrates made up of many sugar monomers linked together
Starch- polymer of glucose, energy source
Glycogen- polymer of glucose, energy storage in liver and muscle cells
Disaccharide- two monosaccharides linked together, require glyosidic linkage
Aldose- has functional group c=o on end
Ketose- has functional group c=o in middle, shape of carbohydrates
Cellulose- polymer of glucose, found in plants, shape of carbohydrates
Chitin- polymer of modified glucose, in animal exoskeletons and cell walls of fungi, strengthen structure
Lipids- molecules with little or no affinity for water, not a polymer
Lactose- glucose+ galactose
Structure of fat- one glycerol, three fatty acids, ester linkages
Function of fats- energy storage, insulating, cushioning
Saturated fat- carbons in carbon tail are fully saturated with hydrogen
Unsaturated fat- carbons are not fully saturated with hydrogen, double bond between two carbon
Trans Fat- human manufactured, partially-hydrogenated, act like saturated fats
Phospholipid structure- amphipathic properties: hydrophobic tail, hydrophilic head
Phospholipid function- structure and regulation, found in cell membranes
Steroid structure- carbon skeleton consisting of four fused rings to which functional groups are attached, cholesterol
Cholesterol function- precursor for hormones, can be changed and modified into other hormones, precursor for vitamin D and bile salts, stabilizes animal membranes
HDL- good cholesterol, picks it off artery walls and carries it to liver
LDL- drops cholesterol in arteries, blocking them
Protein structure- made of amino acids, amino group, carboxyl group, hydrogen, and a side chain that varies
Polypeptide chain- chain of amino acids
Peptide bonds- dehydration reaction between amino acids
Protein Primary structure- amino acid sequence
Protein Secondary structure- repeated coiling and folding
Protein tertiary structure- irregular contortions of molecule, stabilized 3D shape
Protein quaternary structure- 2 or more polypeptide chains that bond together
Protein function- muscle structure and function, enzymes, transportation, embedded in plasma membrane
Denaturation- unfolding of proteins shape
Renaturation- returning protein to original shape
Digression- protein structure can change with a change in temp, pH, etc.
Chaperonin molecules- enable polypeptide to undergo appropriate folding
Mad Cow Disease- an example of protein digression
Nucleic Acids- Polymers of nucleotides (DNA and RNA)
Structure of nucleotide- phosphate group, pentose sugar, nitrogenous base
Pyrimidine- cytosine, thymine, uracil, 1 nitrogenous base
Purine- adenine, guanine, 2 nitrogenous bases
Nucleotide- monomer of nucleic acid
Function of nucleic acids- codes for making proteins, transcription and translation
Created by: mr_spangler



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