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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