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WGU C785 GRADED A+

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What is the basic structure of an amino acid? What do they look like? - amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C), and variable group How do you identify the 3 different types of side chains: non-polar/hydrophobic, polar, and charged? - Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH, SH, or NH. Charged - end with a charge what kinds of bonds do each of the 3 different types of side chains make? - ionic, hydrophobic/non-polar, charged What are the 4 levels of protein structure? - Primary - linear structure, Secondary - Folded into helix or pleated sheet caused by hydrogen bonding, tertiary - 3D structure caused by side chain interactions, quaternary - 1+ amino acid chains combine = multiple subunits MUST have 1+ subunit What enviormental change breaks each type of bond? - hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen - temperature, change in pH, disulfide - reducing agents what type of amino acid side chain leads to protein aggregration? - hydrophobic bonds how do environmental changes affect protein folding? - Extreme temp can cause hydrogen bonds to break apart = malformation of protein folding how do mutations affect protein structure? - Can cause structure to change. Protein loses form = loses function. May form a different protein. What is an electron? - Negatively charged atom on outer ring for bonding What is energy: - Power derived fro chemical interaction what are covalent bonds? - chemical bond, atoms share 1+ valence electrons

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WGU C785 GRADED A+

What is the basic structure of an amino acid? What do they look like? - ✔✔amino group (NH2 or
NH3), carboxyl group (COO or COOH), alpha carbon (C), and variable group



How do you identify the 3 different types of side chains: non-polar/hydrophobic, polar, and charged?
- ✔✔Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH, SH, or NH.
Charged - end with a charge



what kinds of bonds do each of the 3 different types of side chains make? - ✔✔ionic,
hydrophobic/non-polar, charged



What are the 4 levels of protein structure? - ✔✔Primary - linear structure, Secondary - Folded into
helix or pleated sheet caused by hydrogen bonding, tertiary - 3D structure caused by side chain
interactions, quaternary - 1+ amino acid chains combine = multiple subunits MUST have 1+ subunit



What enviormental change breaks each type of bond? - ✔✔hydrophobic - temperature change, ionic
- salt or decreased pH, hydrogen - temperature, change in pH, disulfide - reducing agents



what type of amino acid side chain leads to protein aggregration? - ✔✔hydrophobic bonds



how do environmental changes affect protein folding? - ✔✔Extreme temp can cause hydrogen bonds
to break apart = malformation of protein folding



how do mutations affect protein structure? - ✔✔Can cause structure to change. Protein loses form =
loses function. May form a different protein.



What is an electron? - ✔✔Negatively charged atom on outer ring for bonding



What is energy: - ✔✔Power derived fro chemical interaction



what are covalent bonds? - ✔✔chemical bond, atoms share 1+ valence electrons

,what is an ionic bond? - ✔✔bond between positive and negative



what is a hydrogen bond? - ✔✔weak bond between positive and negative



with an amino? - ✔✔piece of amino acid, NH2 or NH3



what is a carboyxl? - ✔✔piece of amino acid, COO or COOH



What is hydrophobic? - ✔✔Doesn't like water, end with CH



what is hydrophilic? - ✔✔Water Lovering, end with OH, NH, or SH



what is disulfide bond? - ✔✔strongest bond between reduction agents, formed between SH's.



what are zwitterions? - ✔✔amino with positive and negative charges = overall charge of zero



what is a polypeptide - ✔✔polymer of amino acids



What is dehydration synthesis? - ✔✔Process of forming peptide bonds



what is hydrolysis? - ✔✔adding water to destroy bonds



what is an alpha helix? - ✔✔twisted secondary structure, formed by hydrogen bonds



what is a beta sheet? - ✔✔folded second structure shape, formed by hydrogen bonds



what is denaturation? - ✔✔loss of shape duet o interruption of chemical bonds; occurs via extreme
salt, temp, pH



what is aggregation? - ✔✔clumping of inner or outer cellular proteins caused by misfolded proteins
leading to diseases such as Alzheimers, ALS, Parkinson's

, how do enzymes catalyze reactions? - ✔✔bind with substrates to decrease activation energy
required and decrease reaction rate



how do enzymes affect reaction rate and activation energy? - ✔✔decrease activation energy and
decrease reaction rate



what are the 4 steps of the enzymatic cycle? - ✔✔enzyme recognizes substrate, substrate attracts
the enzyme; enzyme-substrate complex is formed; enzyme-product complex formed; product is
released, enzyme recycled



how do environmental changes affect enzymes? - ✔✔High heat, pH change, high salt concentration,
and reducing agents can cause an enzyme to lose its form/lose function



what is a competitive inhibitor? - ✔✔Mimics substrate and takes its place on the active binding site



what is a noncompetitive inhibitor? - ✔✔Binds to allosteric site causing active site to change shape =
preventing substrate from binding with enzyme



what molecules increase/build up or decrease given a specific inhibitor? A -> (enzyme 1) -> B ->
(enzyme 2) -> C -> (enzyme 3) -> D. Pretend Enzyme 2 is inhibited. - ✔✔Inhibitor would cause a build
up for product B, decrease product C. Enzyme 3 and product D would not be created.



what is substrate? - ✔✔the substance on which an enzyme acts



what is a product? - ✔✔result of a reaction



what is an intermediate? - ✔✔products produced in an enzyme pathway before final product



what is an active site? - ✔✔location where substrate binds with enzyme



what is enzyme specificity? - ✔✔Enzymes bind with certain substrate or type of substrate to create a
certain reaction

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