UTA A&P ARANDA EXAM 2 2025/2026 QUESTIONS WITH
SOLUTIONS GRADED A+
✔✔Nonpolar Covalent Bond - ✔✔Equal sharing of electrons between atoms (CO2)
✔✔Polar Covalent Bond - ✔✔Unequal sharing of electrons between two atoms (H2O)
✔✔Hydrogen Bonds - ✔✔Weak attraction electropositive hydrogen of one molecule and
an electronegative atom of another molecule
✔✔Three Main Types of Chemical Reactions - ✔✔Synthesis, Decomposition, Exchange
✔✔Synthesis Reaction - ✔✔Reactions involve atoms or molecules combining to form
larger, more complex molecule (used in anabolic building processes)(A+B->AB)
✔✔Decomposition Reaction - ✔✔reactions involve breakdown of a molecule into
smaller molecules or its constituent atoms (reverse of synthesis, catabolic bondbreaking
reactions)(AB->A+B)
✔✔Exchange Reaction - ✔✔Also called displacement reactions, involve both synthesis
and decomposition (bonds are both made and broken)(AB+C->AC+B and AB+CD-
>AD+CB)
✔✔Exergonic Reaction - ✔✔Releases energy (catabolic)
✔✔Endergonic Reaction - ✔✔Stores energy (anabolic)
✔✔Acids - ✔✔Proton donors: they release hydrogen ions (H+)
✔✔Bases - ✔✔Proton acceptors: they pick up H+ ions (when a base dissolves in
solution, it releases a hydroxyl ion OH-)
✔✔Acidic pH range - ✔✔0-6.99
✔✔Base pH range - ✔✔7.01-14
✔✔Buffers - ✔✔Substances that minimize changes in pH
✔✔Proteins - ✔✔Comprise 20-30% of cell mass, most varied functions of any
molecules
✔✔Proteins contain - ✔✔Carbon, hydrogen, oxygen, nitrogen (sometimes sulfur and
phosphorus)
, ✔✔Peptide Bonds - ✔✔The bonds connecting amino acids together to form polypeptide
chains
✔✔Four protein structural levels - ✔✔Primary structure, secondary structure, tertiary
structure, quaternary structure
✔✔Primary Structure - ✔✔Linear sequence of amino acids (order)
✔✔Secondary Structure - ✔✔How primary amino acids interact with each other (alpha
helix coils resemble a spring, beta pleated sheets resemble accordion ribbons)
✔✔Tertiary Structure - ✔✔How secondary structures interact (one protein folded up on
self and regulated)
✔✔Quaternary Structure - ✔✔How 2 or more different polypeptides interact with each
other (responsible for aggregating structures together, highly functional and highly
regulated)
✔✔Amino Acids - ✔✔20 different types of amino acids; joined by covalent bonds called
peptide bonds ( contain both an amine group and an acid group)
✔✔Fibrous Proteins - ✔✔Strandlike, water-insoluble, and stable; most have tertiary or
quaternary structure; provide mechanical support and tensile strength (keratin, elastin,
collagen)
✔✔Globular Proteins - ✔✔Compact, spherical, water-soluble, and sensitive to
environmental changes; tertiary or quaternary structure; specific functional regions
(antibodies, hormones, molecular chaperones, and enzymes)
✔✔Denaturation - ✔✔Globular proteins unfold and lose their functional, 3-D shape (Can
be caused by decreased pH, or increased temperature)
✔✔Enzymes - ✔✔Globular proteins that act as biological catalysts (lowers the energy
needed to initiate a chemical reaction)
✔✔Holoenzymes - ✔✔Consist of two parts: Apoenzyme (protein portion), cofactor
(metal ion), or coenzyme (organic molecule often a vitamin)
✔✔Three steps involved in the enzyme action - ✔✔1. Substrate binds to enzymes
active site, temporarily forming enzyme-substrate complex
2. Complex undergoes rearrangement of substrate, resulting in final product
3. Product is released from enzyme
SOLUTIONS GRADED A+
✔✔Nonpolar Covalent Bond - ✔✔Equal sharing of electrons between atoms (CO2)
✔✔Polar Covalent Bond - ✔✔Unequal sharing of electrons between two atoms (H2O)
✔✔Hydrogen Bonds - ✔✔Weak attraction electropositive hydrogen of one molecule and
an electronegative atom of another molecule
✔✔Three Main Types of Chemical Reactions - ✔✔Synthesis, Decomposition, Exchange
✔✔Synthesis Reaction - ✔✔Reactions involve atoms or molecules combining to form
larger, more complex molecule (used in anabolic building processes)(A+B->AB)
✔✔Decomposition Reaction - ✔✔reactions involve breakdown of a molecule into
smaller molecules or its constituent atoms (reverse of synthesis, catabolic bondbreaking
reactions)(AB->A+B)
✔✔Exchange Reaction - ✔✔Also called displacement reactions, involve both synthesis
and decomposition (bonds are both made and broken)(AB+C->AC+B and AB+CD-
>AD+CB)
✔✔Exergonic Reaction - ✔✔Releases energy (catabolic)
✔✔Endergonic Reaction - ✔✔Stores energy (anabolic)
✔✔Acids - ✔✔Proton donors: they release hydrogen ions (H+)
✔✔Bases - ✔✔Proton acceptors: they pick up H+ ions (when a base dissolves in
solution, it releases a hydroxyl ion OH-)
✔✔Acidic pH range - ✔✔0-6.99
✔✔Base pH range - ✔✔7.01-14
✔✔Buffers - ✔✔Substances that minimize changes in pH
✔✔Proteins - ✔✔Comprise 20-30% of cell mass, most varied functions of any
molecules
✔✔Proteins contain - ✔✔Carbon, hydrogen, oxygen, nitrogen (sometimes sulfur and
phosphorus)
, ✔✔Peptide Bonds - ✔✔The bonds connecting amino acids together to form polypeptide
chains
✔✔Four protein structural levels - ✔✔Primary structure, secondary structure, tertiary
structure, quaternary structure
✔✔Primary Structure - ✔✔Linear sequence of amino acids (order)
✔✔Secondary Structure - ✔✔How primary amino acids interact with each other (alpha
helix coils resemble a spring, beta pleated sheets resemble accordion ribbons)
✔✔Tertiary Structure - ✔✔How secondary structures interact (one protein folded up on
self and regulated)
✔✔Quaternary Structure - ✔✔How 2 or more different polypeptides interact with each
other (responsible for aggregating structures together, highly functional and highly
regulated)
✔✔Amino Acids - ✔✔20 different types of amino acids; joined by covalent bonds called
peptide bonds ( contain both an amine group and an acid group)
✔✔Fibrous Proteins - ✔✔Strandlike, water-insoluble, and stable; most have tertiary or
quaternary structure; provide mechanical support and tensile strength (keratin, elastin,
collagen)
✔✔Globular Proteins - ✔✔Compact, spherical, water-soluble, and sensitive to
environmental changes; tertiary or quaternary structure; specific functional regions
(antibodies, hormones, molecular chaperones, and enzymes)
✔✔Denaturation - ✔✔Globular proteins unfold and lose their functional, 3-D shape (Can
be caused by decreased pH, or increased temperature)
✔✔Enzymes - ✔✔Globular proteins that act as biological catalysts (lowers the energy
needed to initiate a chemical reaction)
✔✔Holoenzymes - ✔✔Consist of two parts: Apoenzyme (protein portion), cofactor
(metal ion), or coenzyme (organic molecule often a vitamin)
✔✔Three steps involved in the enzyme action - ✔✔1. Substrate binds to enzymes
active site, temporarily forming enzyme-substrate complex
2. Complex undergoes rearrangement of substrate, resulting in final product
3. Product is released from enzyme
