amino acids, peptide bonds, protein structure, enzymes
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
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| show | amino acids
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| an amino acid contains an ____________________, a ____________________, and a side chain of variable structure called an _________________ | show 🗑
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| -NH3+ | show 🗑
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| show | carboxyl group
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| hydrophobic amino acids have _______________ side chains | show 🗑
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| side chains of polar amino acids can interact with water because they contain __________________ groups, including OH, NH, and SH | show 🗑
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| cysteine, the only amino acid with a -SH group is able to form __________________ | show 🗑
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| what are the 2 negative charged amino acids | show 🗑
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| show | 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 | show 🗑
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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 | show 🗑
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| the sequence of amino acids in a polypeptide is called the protein's ____________________. | show 🗑
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| show | alpha helix, beta sheet
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| ______________________ is the localized shape that is formed by hydrogen bonding patterns of amino acid backbone atoms | show 🗑
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| _____________________ is the result of different secondary structures interacting with one another via their R groups. | show 🗑
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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. | show 🗑
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| show | hydrophobic effect
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| show | a slight attraction that happens when non polar groups are close together
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| ionic bond forms between _____________________ side chains | show 🗑
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| ___________________ form when two cysteine groups are in close proximity and the two sulfur atoms form a covalent bond | show 🗑
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| _________________ is the loss of a protein's native 3d structure due primarily to the loss of _________ structure | show 🗑
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| which denaturation technique disrupts hydrophobic interactions | show 🗑
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| show | changes in ph and high salt concentrations
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| which denaturation technique disrupts disulfide bonds | show 🗑
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| show | amyloid-beta
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| show | alpha-synuclein
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| primary structure is held together by ______________ bonds | show 🗑
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| what 4 side chain interactions stabilize the tertiary structure of proteins | show 🗑
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| show | amino; carboxyl
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| show | enzymes
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| show | lowering
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| show | substrate
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| show | phosphorylation
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| show | 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 | show 🗑
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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 | show 🗑
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| show | feedback inhibition
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| in the enzymatic cycle, the enzyme shape is changed when ______________ and resumes its original shape when ______________ after ___________________ | show 🗑
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Created by:
kinseycharles
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