MCB 150 BUNDLED EXAMS EXAM PREP
EXAM STUDY SHEET 2026 ALREADY
PASSED GRADED A+.
⩥ stereoisomers. Answer: have identical bonding relationships, but
the spatial positioning of their atoms differ
⩥ cis isomer. Answer: Carbon chain is found on the same side of the
C=C double bond.
⩥ trans isomer. Answer: carbon chain found on opposite side
⩥ condensation reaction. Answer: reaction in which two or more
molecules are combined into one larger molecule by covalent
bonding, with the loss of a small water molecule
⩥ hydrolysis reaction. Answer: chemical reaction that adds water to
break apart other molecules
⩥ all carbohydrates contain.... Answer: carbon, hydrogen, and oxygen
⩥ carbohydrates. Answer: monomer= monosaccrihdes (simple sugars
like pentose or hexose)
polymer= polysaccrihdes
,energy stored within the bonds
⩥ glycosidic bond. Answer: covalent bond between 2 sugar molecules
via dehydration reaction
⩥ energy storage. Answer: starch= plant cells
glycogen= animal cells
⩥ lipids. Answer: -have no monomers bc they are not polymers
-hydrophobic molecules composed mainly of carbon, hydrogen,
oxygen
-nonpolar, insoluble in water
⩥ triglycerides. Answer: fats formed when glycerol bonds to 3 fatty
acids. a 3 carbon molecule w/ one hydroxyl group
⩥ saturated fatty acid. Answer: fatty acid in which all carbons are
linked by single covalent bonds, solid at room temp
⩥ unsaturated fatty acids. Answer: fatty acids containing one or more
carbon double bonds. (fat stores energy to make ATP) liquid at room
temp
⩥ phospholipid. Answer: a lipid that contains phosphorus and that is a
structural component in cell membranes (backbone)
,⩥ fatty acid chain. Answer: hydrophobic tails
⩥ phosphate group. Answer: hydrophilic head
⩥ steroid. Answer: -lipid containing 4 interconnected rings of carbon
atoms
-hormone in plants and animals
-hydroxyl group attached
⩥ amino acids. Answer: -monomer= AA(CHNOPS)
-polymer= proteins
amino group accepts hydrogen and has a + charge, while carboxyl
loses that hydrogen and has a - charge
⩥ peptide bond. Answer: covalent bond between carboxyl and amino
group that links amino acids in a polypeptide
⩥ N terminus vs. C terminus. Answer: N= location of the first amino
in a polypeptide, the "amino" end
C= location of last amino in polypeptide, carboxyl end
, ⩥ protein structure levels. Answer: 1. primary: linear sequence of
amino acids, determined by genes, carries info for production of
polypeptides
2. secondary
-alpha helix: repeating structure stabilized by hydrogen bonds
-beta sheets: regions lie parallel to each other
3. tertiary: 3D shape of a single polypeptide, involves side chain
interactions
4. quartenary: when 2 polypeptides bond w/ each other
⩥ protein structure bonds. Answer: 1. hydrogen bonds: important in
levels 2,3,4. Large # of weak hydrogen bonds creates strong force for
protein folding and stability
2. ionic bonds/polar interactions: important in 3rd and 4th structure,
some side chains are positively or negatively charged
3. hydrophobic effect: as a protein folds, non polar amino acids are
found in the center of the protein to avoid water. important in 3 and 4
4. van der walls dispersion forces: 3rd structure. occurs when atoms
within molecules have temporary weak attraction if they are optimal
distance apart.
EXAM STUDY SHEET 2026 ALREADY
PASSED GRADED A+.
⩥ stereoisomers. Answer: have identical bonding relationships, but
the spatial positioning of their atoms differ
⩥ cis isomer. Answer: Carbon chain is found on the same side of the
C=C double bond.
⩥ trans isomer. Answer: carbon chain found on opposite side
⩥ condensation reaction. Answer: reaction in which two or more
molecules are combined into one larger molecule by covalent
bonding, with the loss of a small water molecule
⩥ hydrolysis reaction. Answer: chemical reaction that adds water to
break apart other molecules
⩥ all carbohydrates contain.... Answer: carbon, hydrogen, and oxygen
⩥ carbohydrates. Answer: monomer= monosaccrihdes (simple sugars
like pentose or hexose)
polymer= polysaccrihdes
,energy stored within the bonds
⩥ glycosidic bond. Answer: covalent bond between 2 sugar molecules
via dehydration reaction
⩥ energy storage. Answer: starch= plant cells
glycogen= animal cells
⩥ lipids. Answer: -have no monomers bc they are not polymers
-hydrophobic molecules composed mainly of carbon, hydrogen,
oxygen
-nonpolar, insoluble in water
⩥ triglycerides. Answer: fats formed when glycerol bonds to 3 fatty
acids. a 3 carbon molecule w/ one hydroxyl group
⩥ saturated fatty acid. Answer: fatty acid in which all carbons are
linked by single covalent bonds, solid at room temp
⩥ unsaturated fatty acids. Answer: fatty acids containing one or more
carbon double bonds. (fat stores energy to make ATP) liquid at room
temp
⩥ phospholipid. Answer: a lipid that contains phosphorus and that is a
structural component in cell membranes (backbone)
,⩥ fatty acid chain. Answer: hydrophobic tails
⩥ phosphate group. Answer: hydrophilic head
⩥ steroid. Answer: -lipid containing 4 interconnected rings of carbon
atoms
-hormone in plants and animals
-hydroxyl group attached
⩥ amino acids. Answer: -monomer= AA(CHNOPS)
-polymer= proteins
amino group accepts hydrogen and has a + charge, while carboxyl
loses that hydrogen and has a - charge
⩥ peptide bond. Answer: covalent bond between carboxyl and amino
group that links amino acids in a polypeptide
⩥ N terminus vs. C terminus. Answer: N= location of the first amino
in a polypeptide, the "amino" end
C= location of last amino in polypeptide, carboxyl end
, ⩥ protein structure levels. Answer: 1. primary: linear sequence of
amino acids, determined by genes, carries info for production of
polypeptides
2. secondary
-alpha helix: repeating structure stabilized by hydrogen bonds
-beta sheets: regions lie parallel to each other
3. tertiary: 3D shape of a single polypeptide, involves side chain
interactions
4. quartenary: when 2 polypeptides bond w/ each other
⩥ protein structure bonds. Answer: 1. hydrogen bonds: important in
levels 2,3,4. Large # of weak hydrogen bonds creates strong force for
protein folding and stability
2. ionic bonds/polar interactions: important in 3rd and 4th structure,
some side chains are positively or negatively charged
3. hydrophobic effect: as a protein folds, non polar amino acids are
found in the center of the protein to avoid water. important in 3 and 4
4. van der walls dispersion forces: 3rd structure. occurs when atoms
within molecules have temporary weak attraction if they are optimal
distance apart.
