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25 Cards in this Set
- Front
- Back
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purmidines
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-in nucleic acid
-single rings: cytosine (C), thymine (T), Uracil (U) |
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Purines
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-in nucleic acid
-double rings: Adenine (A), Guanine (G) |
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nucleic acids
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-polymers specialized for storage, transmission, and use of genetic information
-DNA and RNA -monomers: nucleotide -complementary binding= Adenine and thymine (A-T), and cytosine and guanine (C-G) |
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nucleotide
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-pentose sugar + N base + phosphate group
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nucleoside
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- pentose sugar + N base
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metabolic pathways
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-product of 1 reaction is a substrate for the next, series of reactions
-first reaction is the commitment step- other reactions then happen in sequence -feedback inhibition the final product acts as a noncompetitive inhibitor or the first enzyme, which shuts down the pathway |
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carbohydrates
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-cho
-sugar molecules -Cn(H2O)n1 -source of energy stored -function of structural molecules give organisms shape ie. store glycogen in plant cellulose -serve as recognition or signaling molecules that trigger specific biological responses -transport stored energy -monomer:simple sugars -> mono saccharides -polymers -> polysaccharides |
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pentoses
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-mono saccharides of cho's
-5 carbon sugars -ribose and deoxyribose are backbones of RNA and DNA |
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hexoses
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-mono saccharides of cho's
-6 carbon sugars -(C6 H12 O6) -include glucose, fructose, mannose, and galactose |
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polysaccharides
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-starch
-glycogen -cellulose |
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proteins
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-polypeptide
-monomers are amino acids linked to form peptide bonds(by covalent) -amino and carboxylic acid functional group -R group differs in each amino acid H3 N+ - C - COO- |
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protein primary structure
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-sequence of amino acids by single peptide bond
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protein secondary structure
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-regular, repeated spatial patterns in different regions, resulting from hydrogen bonding
-alpha helix= right handed coil -beta pleated sheet= 2 or more polypeptide chains are extended and aligned |
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protein tertiary structure
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-polypeptide chain is bent and folded; results in definitive 3-d shape
-outer surfaces present functional groups that can interact with other molecules |
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protein quaternary structure
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-2 or more polypeptide chains bound together by hydrophobic and ionic interactions, and hydrogen bonds
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protein denaturation
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-alterations in pH, salt concentration, temperature, or other environmental factors can cause protein to unravel
-loss of protein's native structure -biologically inactive |
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enzymes
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-organic catalysts are substances that speed up reactions
-all enzymes are proteins but not all proteins are enyzmes -bind to specific substrate by active site -reactants are substrates that bind to specific site on enzyme-the active site |
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cofactors
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-inorganic ions
ie. metal ions |
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coenzymes
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-add or remove chemical group from the substate
-organic -ie. vitamins |
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prosthetic groups
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-(non amino acid groups) permanently bound to their enzymes
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irreversible inhibition
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-regulation of metabolism
-inhibitor covalently binds to side chain in active site -enzyme is permanently inactivated |
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reversible inhibition
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-regulation of metabolism
-competitve inhibitor competes with natural substrate for active site -aggressive -noncompetitive inhibitor binds at site distinct for the active site causing change in enzyme shape and function |
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allosteric regulation
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-regulation of metabolism
-non substrate molecule binds to a site other than active site -enzyme changes shape, which alters chemical attraction of the active site for substrate -can activate or inactivate enzymes |
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dna
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-sugar= deoxyribose
-bases= adenine, cytosine, guanine, thymine -double strand |
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rna
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-sugar=ribose
-bases= adenine, cytosine, guanine, uracil -single strand |
