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WGU BIOCHEM Module 2
amino acids, peptide bonds, protein structure, enzymes
| just as nucleic acids are polymers of nucleotides, proteins are polymers of ______________ | amino acids |
| an amino acid contains an ____________________, a ____________________, and a side chain of variable structure called an _________________ | amino group, carboxyl group, R group |
| -NH3+ | amino group |
| -COO- | carboxyl group |
| 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 |
| side chains of polar amino acids can interact with water because they contain __________________ groups, including OH, NH, and SH | hydrogen-bonding |
| cysteine, the only amino acid with a -SH group is able to form __________________ | disulfide bonds |
| what are the 2 negative charged amino acids | aspartate, glutamate |
| what are the 2 positive charged amino acids | lysine, arginine |
| 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 |
| a peptide bond can be broken down by ____________ in which water is added back to the bond and separates the two amino acids | hydrolysis |
| the sequence of amino acids in a polypeptide is called the protein's ____________________. | primary structure |
| the most common secondary structures are the ____________ and ____________ | alpha helix, beta sheet |
| ______________________ is the localized shape that is formed by hydrogen bonding patterns of amino acid backbone atoms | secondary structure |
| _____________________ is the result of different secondary structures interacting with one another via their R groups. | tertiary structure |
| 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 |
| 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 |
| hydrophobic interactions | a slight attraction that happens when non polar groups are close together |
| ionic bond forms between _____________________ side chains | oppositely charged |
| ___________________ form when two cysteine groups are in close proximity and the two sulfur atoms form a covalent bond | disulfide bond |
| _________________ is the loss of a protein's native 3d structure due primarily to the loss of _________ structure | denaturation; tertiary |
| which denaturation technique disrupts hydrophobic interactions | heat |
| which 2 denaturation technique disrupts ionic bonds and hydrogen bonds | changes in ph and high salt concentrations |
| which denaturation technique disrupts disulfide bonds | reducing agents (perm) |
| 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 |
| in parkinson's disease, neurons in a portion of the brain accumulate fragments of a protein known as __________________ | alpha-synuclein |
| primary structure is held together by ______________ bonds | peptide |
| what 4 side chain interactions stabilize the tertiary structure of proteins | ion pairs, hydrophobic interactions, hydrogen bonds, disulfide bonds |
| peptide bonds are formed between the __________ group and the ____________ group | amino; carboxyl |
| ______________ are protein catalysts that can do the same reaction over and over | enzymes |
| enzymes speed up chemical reactions by __________the activation energy of a reaction | lowering |
| a _________ is a molecule that an enzyme will bind preferentially to any other molecule | substrate |
| _________________ modifies enzyme activity by either turning it on or off | phosphorylation |
| ____________ add phosphate groups to proteins while ____________ remove them | kinases, phosphatases |
| 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 |
| ________________ attach to the enzyme at an allosteric site, distorting the tertiary protein structure and altering the shape of the active site | noncompetitive inhibitor |
| _____________________, a kind of reversible noncompetitive inhibition regulates the rate of many metabolic pathways | feedback inhibition |
| 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 |
Created by:
kinseycharles
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