amino acids, peptide bonds, protein structure, enzymes
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| just as nucleic acids are polymers of nucleotides, proteins are polymers of ______________ | amino acids
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| an amino acid contains an ____________________, a ____________________, and a side chain of variable structure called an _________________ | amino group, carboxyl group, R group
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| -NH3+ | amino group
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| -COO- | carboxyl group
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| hydrophobic amino acids have _______________ side chains | nonpolar; C-C and c-H bonds that cannot form hydrogen bonds; interact weakly with water; like to be interior
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| side chains of polar amino acids can interact with water because they contain __________________ groups, including OH, NH, and SH | hydrogen-bonding
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| cysteine, the only amino acid with a -SH group is able to form __________________ | disulfide bonds
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| what are the 2 negative charged amino acids | aspartate, glutamate
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| what are the 2 positive charged amino acids | lysine, arginine
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| the formation of a peptide bond involves the _______________________ of the carbonyl group of one amino acid and the amino group of another amino acid | dehydration
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| a peptide bond can be broken down by ____________ in which water is added back to the bond and separates the two amino acids | hydrolysis
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| the sequence of amino acids in a polypeptide is called the protein's ____________________. | primary structure
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| the most common secondary structures are the ____________ and ____________ | alpha helix, beta sheet
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| ______________________ is the localized shape that is formed by hydrogen bonding patterns of amino acid backbone atoms | secondary structure
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| _____________________ is the result of different secondary structures interacting with one another via their R groups. | tertiary structure
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| proteins with more than one polypeptide have ________________, and the polypeptides are held together by R group interactions similar to those that stabilize tertiary structure. | quaternary strucutre
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| the largest force governing protein structure is the __________________, which causes R groups to cluster together in the interior of a protein in order to minimize their contact with water | hydrophobic effect
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| hydrophobic interactions | a slight attraction that happens when non polar groups are close together
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| ionic bond forms between _____________________ side chains | oppositely charged
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| ___________________ form when two cysteine groups are in close proximity and the two sulfur atoms form a covalent bond | disulfide bond
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| _________________ is the loss of a protein's native 3d structure due primarily to the loss of _________ structure | denaturation; tertiary
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| which denaturation technique disrupts hydrophobic interactions | heat
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| which 2 denaturation technique disrupts ionic bonds and hydrogen bonds | changes in ph and high salt concentrations
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| which denaturation technique disrupts disulfide bonds | reducing agents (perm)
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| the extracellular amyloid material in alzheimer's disease consists primarily of a protein called _____________, a small fragment of a larger precursor protein located in the cell membrane | amyloid-beta
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| in parkinson's disease, neurons in a portion of the brain accumulate fragments of a protein known as __________________ | alpha-synuclein
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| primary structure is held together by ______________ bonds | peptide
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| what 4 side chain interactions stabilize the tertiary structure of proteins | ion pairs, hydrophobic interactions, hydrogen bonds, disulfide bonds
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| peptide bonds are formed between the __________ group and the ____________ group | amino; carboxyl
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| ______________ are protein catalysts that can do the same reaction over and over | enzymes
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| enzymes speed up chemical reactions by __________the activation energy of a reaction | lowering
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| a _________ is a molecule that an enzyme will bind preferentially to any other molecule | substrate
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| _________________ modifies enzyme activity by either turning it on or off | phosphorylation
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| ____________ add phosphate groups to proteins while ____________ remove them | kinases, phosphatases
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| a ____________________ is usually a molecule similar in structure to a substrate that can bind to an enzyme's active site even though the molecule is unable to react | competitive inhibitor
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| ________________ attach to the enzyme at an allosteric site, distorting the tertiary protein structure and altering the shape of the active site | noncompetitive inhibitor
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| _____________________, a kind of reversible noncompetitive inhibition regulates the rate of many metabolic pathways | feedback inhibition
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| in the enzymatic cycle, the enzyme shape is changed when ______________ and resumes its original shape when ______________ after ___________________ | substrate binds; product is released; substrate is converted to product
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