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45 Cards in this Set
- Front
- Back
Proteins
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Are polymers made up of 20 different amino acids
Functions: -Enzymes - catalyze a reaction/speed it up -Defensive proteins (antibodies) - kill bacteria, defend your body -Hormonal/regulatory proteins -Receptor proteins - receive and respond to molecular signals -Storage proteins - store amino acids -Structural proteins -transport proteins -genetic regulatory proteins -Can consist of more than one type of polypeptide chains -Bind noncovalently with specific molecules |
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Carbohydrates
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Sugar monomers (monosaccharides)
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Nucleic Acids
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4 kinds of nucleotide monomers
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Lipids
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fatty acids
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Macromolecules
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polymers with with molecule weights greater than 1,000
-may contain many different functional groups |
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Functional groups
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direct interactions/functions
-group of atoms with specific chemical properties and consistent behavior. -Some are polar, some are acidic, etc |
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Isomers
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molecules with the same chemical formula but they look different
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Optical Isomers
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4 different atoms attached with it
- some biochemical molecules that can interact with one optical isomer are unable to "fit" the other |
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Biochemical Unity
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macromolecules are present in the same proportions in all living organisms have similar functions
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Polymer
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a large molecule made up of monomers
- polymers are broken down into monomers in hydrolysis reactions |
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Monomer
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a small molecule that forms polymers
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Condensation reaction
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chemical reaction in which two molecules become connected by a covalent bond and a molecule of water is released
-makes polymers - monomers are joined by covalent bonds |
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Structural Isomers
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molecules made up of the same kinds and numbers of atoms in which the atoms are bonded differently
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Polypeptide Chains
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unbranched (linear) polymers of covalent linked amino acids
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Amino Acids
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Have carboxyl and amino groups - function as both acid and base
-can be grouped based on side chains - bond covalently Exist in two isomeric forms: D-amino acid (dextro, "right") - can be found in bacteria L-amino acids (levi, "left") - is found in organisms |
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Side chains
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(R-groups)
also have functional groups |
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Primary structure
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the sequence of amino acids
- determines secondary and tertiary structure - how the protein is. |
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Secondary structure
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a helix - right-handed coil resulting from hydrogen bonding between N-H group bonds
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Tertiary
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bending and folding
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Denature
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changing the shape of a protein
by heat: changes in pH, non polar substances if cooled: protein goes back to original form (depends) |
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Quaternary structure
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results from the interaction of subunits
Each subunit has its own unique tertiary structure |
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Proteins sometimes bind to the wrong molecules
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-after denaturation
-when they are new and still unfolded |
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Chaperones
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a protein that guards other proteins by counteracting molecular interactions that threaten their three-dimensional structure
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Heat shock proteins (HSPs)
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Chaperone proteins expressed in cells exposed to high or low temperatures or other forms of environmental stress
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Carbohydrates
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-Source of stored energy
-Transport stored energy -Carbon skeletons for many other molecules |
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Monosaccharides
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Simple sugars
-Have different numbers of carbons: -Hexoses: six carbons - structural isomers -Pentoses: five carbons -Bind together in condensation reactions and form glycosidic linkages |
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Disccharides
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two simple sugars linked by covalent bonds
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Oligosaccharides
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three to 20 monosaccharides
-May include other functional groups -often covalently bonded to proteins and lipids |
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Polysaccharides
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More than 20monosaccharides - starch, glycogen, cellulose
-giant polymers of monosaccharides Starch = storage of glucose in plants Glycogen = Cellulose: very stable, good for structural components |
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Glucose
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Cells use this as an energy source
-exists as a straight chain or ring form |
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Glycosidic Linkages
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Bond between carbohydrate (sugar) molecules through an intervening oxygen atom
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Carbohydrates can be...
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modified by adding functional groups:
-sugar phosphate -Amino sugars -Chitin |
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Lipids
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Nonpolar hydrocarboms
-van der Waals forces hold them together -Not polymers, not covalently bonded -Fats and oils store energy -Phospholipids -Carotenoids and chlorophylls -Steroids and modified fatty acids -Animal fat -Nerve insulation -oil and wax on skin, fur, and feathers repels water |
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Phospholipids
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Structural role in cell membranes
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Fats and oils
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triglycerides (simple lipids)
-composed of fatty aids and glycerol |
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Glycerol
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3 - OH groups (an alcohol)
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Fatty Acid
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nonpolar hydrocarbon with a polar carboxyl group
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Ester Linkage
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carboxyls bond with hydroxyls of glycerol
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Saturated fatty acids
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no double bonds between carbons
-Animal fats are usually saturated because they're packed together tightly, and they're solids at room temperature |
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Unsaturated fatty acids
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some double bonds in carbon chain
monounsaturated: polyunsaturated: |
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Amphipathic
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having both hydrophilic and hydrophobic regions
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Phospholipids
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fatty acids bound to glycerol
--hydrophilic - the "head" -hydrophobic - "tails" are fatty acid chains -amphipathic |
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Bilayer
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a structure that is two layers in thickness
-the phospholipid layer of membranes |
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Vitamins
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Small molecules not synthesized by the body
-acquired in diet |
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Waxes
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highly non polar and impermeable to water
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