CHEM210 / CHEM 210 Module 6: (Latest Update
2026 / 2027) Organic Chemistry | Questions &
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Q: What is the difference between a nucleoside and nucleotide?
Answer
A nucleoside is formed from the covalent bonding of a base (purine or pyrimidine) to
either ribose (RNA) or 2-deoxyribose (DNA). Nucleotides are built from a nitrogen
containing organic base, a monosaccharide, and phosphate.
Q: What characteristic makes purines and pyrimidine heterocyclic?
Answer
Each has a ring with nitrogen in the ring instead of all carbon atoms in the ring.
Q: Is this molecule ribose or 2-deoxyribose? Briefly explain what structural
information was used to determine this.
Answer
Ribose. This molecule contains an -OH on carbon 2. 2-deoxyribose has an -H atom on
the second carbon.
Q: Is the following a pyrimidine or purine? Provide the name and one-letter symbol.
Answer
Pyrimidine. It is thymine (T).
Q: What is the difference between thymine and uracil?
Answer
These two bases differ by a methyl group. Thymine has an extra methyl group on the
ring.
Q: From the course and module information, where in a eukaryotic or prokaryotic cell,
is the DNA located? How about the RNA?
Answer
DNA is located in the nucleus of a eukaryotic cell or the nucleoid of a prokaryotic cell.
RNA is found in the nucleus, on the ribosome, and in other parts of the cell.
Q: Which DNA and RNA bases contain a carbonyl group?
Answer
Guanine, cytosine, thymine, and uracil all contain C=O group attached to the rings.
Adenine is the only base that does not.
Q: What constitutes the backbone of DNA?
Answer
In DNA, this consists of the alternating deoxyribose and phosphate groups linked
together through covalent bonds.
Q: How many hydrogen bonds form between A and T?
Answer
Two hydrogen bonds are formed between these two bases. G and C form three H-bonds.
Q: Which nucleic acid is single-stranded?
Answer
RNA. RNA forms single strands. (Particularly, this was noted in this module for tRNA.)
DNA forms a double helix.
Q: What interactions stabilize the DNA double helix?
Answer
Hydrogen bonds stabilize the helix. Each AT pair and form two hydrogen bonds, and
each GC pair forms three hydrogens that stabilize the helix, permitting it to maintain
this shape.
Q: What type of RNA has a sequence that is complementary to DNA?
Answer
mRNA is complementary so that it can transmit the information to the ribosome.
Q: Which has the largest molecular weight chains: mRNA, tRNA, or rRNA?
Answer
rRNA. These molecules make up ribosomes.
Q: What structural forms of DNA have a right-handed helix? Which form has a left
handed helix?
Answer
The A- and B-forms are right-handed, while the Z-form is left-handed.
Q: What function does cAMP perform in cells?
Answer
cAMP is a communication molecule in cellular signaling. It acts as a secondary
messenger.
Q: In DNA, adenine always pairs with ________.
- Thymine - Guanine - Uracil - Cytosine
Answer - Thymine
Q: DNA is built from which of the following?
- Nucleosides - Genes - Purines - Nucleotide - Codons
Answer - Nucleotide
Q: The double helix of DNA is stabilized mainly by __________.
- Ionic bonds - Covalent bonds - Ion-dipole bonds - Hydrogen bonds - Hydrogen covalent bonds
Answer - Hydrogen bonds
Q: Which of the following pentose sugars is a constituent of DNA?
- Xylose - Ribitol - 2-deoxyribose - Arabinose - Ribose
Answer - 2-deoxyribose
Q: Pyrimidines have ________ ring(s), (each) containing ______ nitrogen(s),
whereas purines have ________ ring(s), (each) containing ______ nitrogen(s).
- 1; 1; 1; 1 - 1; 2; 2; 2
- 2; 2; 1; 2 - 2; 1; 1; 2 - 2; 2; 1; 1
Answer - 1; 2; 2; 2
Q: Identify the base guanine from among the following structures.
Answer
5 NH in rings with a double bonded O
Q: Which of the following nucleic acids is responsible for using the encoded genetic
information to produce of proteins found in living organisms?
- Peptide nucleic acid - Ribonucleic acid - Ribitol nucleic acid - Deoxyribonucleic acid - Glycerol nucleic acid
Answer - Ribonucleic acid
Q: Identify the complementary bases from the following.
- Adenine-Cytosine
- Adenine- Thymine - Guanine-Thymine - Guanine-Adenine - Cytosine-Uracil
Answer - Adenine- Thymine
How many hydrogen bonds are made between G and its complementary nucleotide?
CHEM210 / CHEM 210 Module 4: (Latest Update
2026 / 2027) Organic Chemistry | Questions &
Answers | Grade A | 100% Correct – Portage
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Q: Glycerol contains how many carbon atoms?
- 3 - 4 - 5 - 15
Answer - 3
Q: Which of the following are derived from or made from fatty acids?
- Cholesterol - Carotenoids - Phosphoglycerides - Both A and B - Both A and C
Answer - Phosphoglycerides
Q: Triacylglycerols are made from a ________ and ________.
- glycerol; cholesterol Correct! - glycerol; three fatty acids - ceramide; three fatty acids - ceramide; three cholesterols - carotenoid; two cholesterols
Answer - glycerol; three fatty acids
Q: PUFA
polyunsaturated fatty acid
Answer - 2 or more double bonds
Q: A ________ is a carboxylic acid that is a structural component of lipids.
- Amino acid - Carotenoid - Sphingolipid - cholesterol
- None of the above
Answer - None of the above
Q: A particular lipid is a liquid at room temperature, so it is called a(n) ________.
- Oil - Fat - Lipid - Membrane - Sphingolipid
Answer - Oil
Q: ________ are a class of membrane proteins that are loosely associated with the
membrane bilayer.
- Transmembrane protein - Integral protein - Channel protein - Transport protein - Peripheral protein
Answer - Peripheral protein
Q: Isoprene units are used to make all of the following except __________.
A. Fatty acids
B. Carotenoid molecules
C. Sphingolipids
D. Both B and C
E. All of the above
Answer
A. Fatty acids
Q: Which notation is for a fatty acid with one double bond?
A) 18:1( Δ 12)
B) 1:18
( C) 1:12
( D) 2:18
( E) 12:1(7,9)
Answer
A) 18:1( Δ 12)
Q: Which notation indicates a 14-carbon omega-3 fatty acid that contains no other
double bonds?
A) 14:1 Δ 11)
( B) 17:1 Δ 14)
( C) 14:1 Δ3)
( D) 13:1(Δ11)
E) 14:0( Δ 11)
Answer
A) 14:1 Δ 11)
Q: __________ is used as the backbone molecule in the formation of storage fats.
- Ceramide - Glucose - Sphingolipid - Glycerol - Phosphoglycerol
Answer - Glycerol
Q: __________ molecules determine blood type in humans.
- Sphingolipids - Triacylglycerols - Cholesterol - Phosphoglycerides - carotenoid
Answer - Sphingolipids
Q: ________ are found in high concentrations in the membranes of the myelin
sheath.
- Fatty acids - Cholesterol - Triacylglycerols - Sphingolipids - Vitamin K molecules
Answer
- Sphingolipids
Q: In a sphingolipid, the fatty acids are attached at carbon-2 by this type of linkage?
- Amide linkage - An ether linkage - An alcohol linkage - A peptide linkage - Alkyl linkage
Answer - Amide linkage
Q: Membrane proteins:
- Are sometimes peripheral - Are sometimes integral
CHEM210 / CHEM 210 Module 3: (Latest Update
2026 / 2027) Organic Chemistry | Questions &
Answers | Grade A | 100% Correct – Portage
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Q: True or False: the amino acids serine and methionine both contain sulfur atoms.
Answer
false
Q: True or False: The following secondary structure shown below is an example of a
beta-turn.
Answer
False
Q: True or False: The side chain of proline is bonded to the backbone nitrogen atom.
Answer
True
Q: True or False: The name of the molecule that binds to an enzyme is called the
apoenzyme.
Answer
False
Q: True or False: An inhibitor that binds at the active site is an uncompetitive
inhibitor.
Answer
False
Q: Which amino acids differ by only one atom?
Ser and Thr
Leu and Ile
Ala and Ser
Asp and Asn
Ser and Cys
Answer
Ser and Cys
Q: The formation of a peptide bond between two amino acids is an example of a(n)
________ reaction.
Answer
Condensation
Q: The peptide Ala-Glu-Gly-Ala-Leu-Arg has __________.
A disulfide bond
Five peptide bonds
Four peptide bonds
A proline residue
No C-Terminal
Answer
Five peptide bonds
Q: Formally, when there are 100 or more amino acids covalently linked together that
is called a __________.
Answer
Protein
Q: What is used by biochemists to indicate the mass of a protein?
Answer
kDa or Da
Q: All of the 20 standard amino acids contain an R-group that is attached to the:
Answer
Alpha Carbon
Q: Which of the following correctly matches the amino acid with its one letter
abbreviation?
Glutamic acid, E
Isoleucine, S
Lysine, L
Phenylalanine, P
Arginine, A
Answer
Glutamic Acid, E or Aspartic Acid, D
Q: The order of amino acids in a protein is written_________.
Answer
N to C-Terminus
Q: Roughly how many amino acids are there in one turn of an alpha helix?
Answer
3.6
Q: In an alpha helix, the R groups on the amino acid residues:
Answer
are found on the outside of the helix spiral
Q: Motifs are classified primarily by their:
Answer
Content and arrangement of the secondary structure
Q: A single folded polypeptide has a globular shape, which describes its
______________ structure.
Answer
Tertiary
Q: How many classes of enzymes are recognized by the IUBMB?
Answer
6
Q: An enzyme requires Cr+3 for catalysis. When the enzyme contains the Cr+3 its
called a(n) ________________.
Answer
Holoenzyme
Q: When a substrate has just started its conversion to a new molecule, it is said to be
in the ______________.
Answer
Transition state
Q: Which of the following would change the rate of an enzyme-catalyzed reaction?
Amino acids, concentration, temp
ph, concentration, temp
ph, polarity, concentration
polarity, concentration, temp
ph, polarity, temp
Answer
ph, concentration, temp
Q: The concept of induced fit refers to the fact that:
Answer
Substrate binding induces a conformation change in the enzyme
Q: The ES stands for:
Answer
Enzyme substrate
Q: any molecule or ion that is necessary for an enzymes function is called a
___________.
Answer
cofactor
Q: Is the following protein globular or fibrous? Explain. Also identify the types of
secondary structures present in the following protein.
Answer
Its a globular protein due to its ball-like shape. Fibrous proteins are long and extended.
The types of secondary structures present are alpha helices, beta sheets and turns.
There are collections of protein structure that fit between true secondary and true
tertiary structure. what is the name of the collections of protein structure? explain the
type of structure.
Answer
Motifs occupy a position between secondary and tertiary. motifs are particularly stable
arrangements of secondary structure, including the connections between them. motifs
are found in a variety of proteins from across all organisms.
What is the lowest level of protein structure? How do scientists communicate
information about this level?
Answer
the primary level is the order of amino acids covalently bonded together including
disulfide bonds, in a polypeptide chain. the primary sequence is written for proteins
from n to c terminal using the one letter or three letter abbreviations.
What is the spot on an enzyme where reactions take place? Explain the characteristics of
this spot.
Answer
the spot of the enzyme where catalysis takes place. this area is often small when
compared to the overall size of the protein. in fact about 10 amino acids make up the
active site.
The secondary structure shown below is an example of a(n):
Answer
Parallel beta sheet
Staphylokinase is said to be a dimer. What is a dimer? Structurally a dimer describes
what level of protein structure?
Answer
A dimer contains two polypeptide chains interacting covalently. This describes the
quaternary structure which has two or more polypeptide chains.
Why are proteins the most important macromolecule?
Answer
They perform most of the work in cells.
How many different proteins are found in humans?
Answer
At least 20,000 different proteins
What are some functions of proteins?
Transport
Hormones
Catalysis
Structure
Protection
Answer
Transport
Proteins help to move molecules around the cell and organism.
i.e. hemoglobin - blood based protein that carries oxygen from the lungs to the tissues
Hormones
these molecules communicate messages between cells
i.e. relaxin - a protein that helps women during childbirth by relaxing pelvic ligaments to
make delivery easier
Catalysis (proteins also known as enzymes)
speed up chemical reactions
i.e. protease - breaks down proteins in cells and help organisms recycle unneeded
proteins; also added to laundry detergent to degrade stains with protein (blood, food)
Structure
give strength to cells, organelles, and tissues
i.e. collagen - found in cartilage, skin, and tendons
Protection
ability to fight foreign invaders (outside proteins and toxins)
i.e. antibodies
Amino acids
monomers used as building blocks
contain both an amine functional group and a carboxylic acid functional group; both
functional groups are connected to an alpha carbon
What permits all amino acids to link together in a protein?
each amino acid has the same HN3, CH, COO- groups
What makes amino acids unique?
the unique part of each amino acid is indicated by the R, which is called the side chain
side chains differ in composition, size, and charge
while each amino acid has a different side chain, they can be classified by their
commonality in structure
its is common to group the side chains by charge, size, and polarity
True or False: All proteins are constructed from the same 20 amino acids
True
What is physiological pH?
7.4
Non-polar aliphatic (straight chain amino acids)
relatively small - permits them to interact with other groups
found in the interior of the protein, away from water, nestled with other aliphatic groups
*Proline is a unique amino acid that deviates from the general structure as the side
chain bonds to the backbone N; only amino acid with this type of structure (not flexible -
advantage and disadvantage in protein structure)
Non-polar aromatic group of amino acids
similar to aliphatic in that they are non-polar, but the side chains of these compounds
contain a ring of carbons as an aromatic functional group
more rigid and not as small as the aliphatic group
Polar, but neutral amino acids
contain side chains that have a dipole, and most can H-bond
this permits these amino acids to interact strongly with water and are often found on the
outside of the protein and in contact with water
Acidic amino acids
have side chains with pKa values smaller than 7, which indicates they lose their proton
in the acidic pH range
this property also means that at physiological pH these amino acids are negatively
charged
Basic amino acids
have a pKa that is near or greater than 7, which means their side chains are normally
positively charged
these molecules are often found in contact with water because they H-bond
they are often located near acidic residues in proteins to take advantage of favorable
interactions between positive and negative charges
Histidine
does not have a charged group on its side chain
At a slightly lower pH, it would appear as depicted - the pKa of the side HN+ group
(indicated by the double dagger) is 6.00, so it typically has no charge at pH 7.4
True or False: cysteine is a unique amino acid that is neutral and polar with an
uncharged side chain that can form disulfide bonds by their sulfur atoms covalently
bonding
True
disulfide bonds
stabilize a protein structure when present
not all proteins contain these bonds, but they are common in proteins that exist outside
of the cell
i.e. keratin - protein component of hair; straight or curly hair holds its shape through
disulfide cross linking between strands of hair, these bonds are strong which permits
hair to maintain its shape
polypeptides
long chains of amino acids (99 residues or less)
True or False: As macromolecules, proteins are synthesized from an average of 100 to
300 amino acids into a large chain
True
What dictates the exact sequence of amino acids?
cell's DNA
Where does synthesis of proteins occur?
in the ribosomes, amino acids are covalently linked together to form a protein in a
highly coordinated process
Synthesis reaction of amino acids
the same reaction for each amino acid occurs b/c of the functional groups common to
each amino acid
the amino functional group of one amino acid reacts with the carboxylic acid functional
group of a second resulting in the two monomers joining together to produce a
dipeptide with the release of water --> condensation rxn since one O from the carboxylic
acid group and 2 H from the amino group are lost as water
What kind of bond is formed between two amino acids?
Peptide bond
the ends of the dipeptide formed have reactive amine and carboxylic groups, which
permit them to form additional peptide bonds
peptide/oligopeptide
describes a short chain of amino acids usually from two to twenty amino acids
has an amino-terminal end (N-terminal end) and a carboxylic-terminal end (C-terminal
end)
protein backbone
all the peptide bonds in a protein which link all the amino acids together
residues
term used to refer to the molecule remaining after the condensation rxn takes place
what classifies a molecule as a protein instead of a polypeptide?
100 residues
What is the mass for a protein that has 100 amino acids?
10,000 g/mol (Da - Dalton) or 10 kDa
supramolecular chemistry
the chemistry of large compounds
conformation
3D structure of proteins
biologically active conformational structures
most proteins adopt a conformation that, when folded, is either fibrous or globular
True or False: shape is important to function when adopting a specific conformation.
True
intrinsically disordered
portions of proteins may exist in a random conformation
What are the four standard levels of protein structure?
1. Primary
2. Secondary
3. Tertiary
4. Quaternary
Primary Structure
refers to the order of amino acids covalently bonded together, including disulfide bonds,
in a polypeptide chain
True or False: scientists routinely use the one-letter abbreviations to show amino acid
sequence.
True
i.e. the first 60 amino acids in the sequence for insulin depicted
Scientists write the sequence, starting with the N-terminal amino acid residue on the
left, and continue writing the sequence to the right in the direction of the C-terminal
True or False: proteins contain at least 100 amino acids, but they may contain
thousands of residues in one chain
True
How do scientists write out the sequence of a protein?
Secondary Structure
used to examine the local 3D structure of amino acid residues close in linear sequence;
there are 3 types of secondary structures
(3) beta-turns
Secondary Structure - alpha helices
(1) alpha-helices: coiled structures where the backbone atoms form H-bonds to stabilize
this sequence; standard helix has 3.6 amino acids/residues per each "turn" while rising
5.4 angstroms per turn (1 angstrom = 1x10-10m); interior of helix has no space; side
chains (R groups) point out of the helix so they can interact with water and other
chemical species
Secondary structure - beta-sheets
(2) beta-sheets: repetitive sheet-like structure; zig-zag orientation that puts adjacent
side chain groups as far apart as possible; formed by individual beta-strands that
interact by H-bonding to one another; parallel and anti-parallel
anti-parallel forms when one beta-strand ends and the amino acid sequence turns back
around on itself, then an additional beta-strand can join other strands to form anti
parallel sheets parallel beta-sheets have beta-strands going in the same direction
differences: H-bonding partners are different and the distance of each repeat is unique -
parallel repeats every 6.5A while the anti-parallel repeats every 7.0A
True or False: About 30% of amino acids are found in turns
True
these turns are changes in the direction of the N and C terminals of the primary
sequence
these turns permit proteins to form secondary structures immediately next to one
another
secondary structure - beta turn
a four-residue unit that turns 180 degrees
the turn is seen as a "rope" connecting the two strands
beta-turns can form with both the alpha helix and beta sheet
motif
collection of particularly stable groups of secondary structures
occupy a position b/w secondary and tertiary structures but are not one of the four
levels specified by scientists
i.e. helix-turn-helix composed of an Alpha helix, followed by a turn, and then another
alpha helix
Tertiary structure
the overall 3D structure of the folded polypeptide
non-covalent forces and disulfide bonds maintain tertiary structure in the proper
conformation necessary for function
i.e. myoglobin depicted is critical for our muscle cells for binding and storing O2
prosthetic group
a non-amino acid portion of the molecule necessary for the structure and function of the
protein
fibrous protein
exists in a long, extended structure of alpha helices
quaternary structure
describes macromolecules that have two or more independent polypeptide chains
associated with one another, the number and orientation of these independent chains
constitute the quaternary structure
i.e. staphylokinase, hemoglobin
Dimer
two polypeptides (two subunits)
tetramer
protein with 4 subunits
-in ending
used for proteins that are not enzymes
i.e. hemoglobin, myoglobin
-ase ending
used for proteins that are enzymes
i.e. protease, staphylokinase
enzymes
proteins that accelerate/speed up chemical reactions
have a high specificity for one molecule, or a collection of molecules, due to their
structure (conformation)
How to enzymes speed up chemical reactions?
reactants bind to the enzyme, primarily in the interior, and then undergo a chemical
transformation
this binding helps to speed the reaction along by lowering the energy needed to get the
reaction started
enzymes do this better than inorganic catalysts due to their complementary structure
the result is that reactions speed up 1000 times or more compared to the rate of
uncatalyzed reactions
substrate
the chemical species that bind to the enzyme and are converted to another compound
lyase
catalyze the forming or breaking of double bonds
oxidoreductases
catalyze oxidation and reduction reactions
i.e. luciferase found in lightning bugs
transferals
catalyze the transfer of a group from one molecule to a second
hydrolases
catalyze the breaking, or hydrolysis, of bonds
isomerases
catalyze the rearrangement within a single molecule
ligases
catalyze the joining of two molecules, or two parts of a molecule
How many classes of enzymes exist?
6
co-factor
non-protein components that are critical for activity
i.e. metal ions such as fumerase requires Mg2+ for activity
coenzymes
organic compounds that function as cofactors; aid enzymes by assisting in the transfer
of chemical groups from one compound to a second
i.e. Vit C, niacin
apoenzyme
an enzyme without the cofactor (either ion or coenzyme)
holoenzyme
when the cofactor is added to the apoenzyme to produce a functional enzyme
active site
specific spot on the enzyme where catalysis takes place
composed of 10 amino acids that form non-covalent interactions with the substrate
which helps to generate a favorable energy change to enhance the reaction
induced fit
small movements of the amino acids in the enzyme to bind specifically to the substrate
interactions at the active site of the enzyme that provide energy to change the
conformation of the enzyme to accommodate the substrate
transition state
the structure of the molecule in its transition into a new molecule
most unstable part of the reaction d/t high potential energy
true or false: increasing the concentration of enzyme generally increases the rate of the
reaction
true
True or False: unfolding renders the enzyme inactive, which means it does not catalyze a
reaction
True
What is the optimal temperature for human function?
37 degrees celsius
inhibitors
slow down or stop enzyme reactions by binding to the enzyme via non-covalent
interactions; reversible inhibitors
1. competitive
2.uncompetitive
3.mixed
CHEM210 / CHEM 210 Module 2: (Latest Update
2026 / 2027) Organic Chemistry | Questions &
Answers | Grade A | 100% Correct – Portage
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Q: Which of the following mol- ecules can form a hydrogen bond?
A. HBr
B. HCl
C. NH3
D. CH4
E. H2
Answer
C. NH3
Q: The pH of a solution of 0.0010 M
NaOH is:
A. 1
B. 11
C. 8
D. 0
E. 14
Answer
B.11
1.0 x 10^-14 = [H+][OH-]
1.0 x 10^-14 = [H+][0.0010]
1.0 x 10^-14 /0.0010
1.0 x 10^-11 = H+
pH = -log[1.0 x 10^-11] = 11
Q: The pH of a solution of 8.9 x 10-12M NaOH is:
A. 8.9
B. 8.9 x 10^-12
C. 4.8
D. 11
E.2.9
Answer
E. 2.9
Kw=[H+][OH-]
1.0 x 10^-14= [H+][8.9 x 10^-12]
[H+]=890
pH=-log[890]
2.9
Q: The pH of a solution of 3.2 x 10^-10 M NaOH is:
A. 3.7
B. 3.7 x 10^-10
C. 4.5
D. 13
E. 8.7
Answer
C. 4.5
1.0 x 10^-14 = [H+][OH-]
1.0 x 10^-14 = [H+][3.2 x 10^-10]
1.0 x 10^-14/3.2 x 10^-10 = [H+]
3.25 x 10^-5 = [H+]
pH = -log [H+]
pH = -log [3.25 x 10^-5]
pH = 4.5
Q: Water is a unique molecule. Which of the following con- tributes to water's unique
place in the chemical world?
A. The geometry of the molecule
B. The polarity of the O-H bonds
C. The ability of water molecules to hydrogen bond
D. The bond angle of water
E. All of the answers are correct
Answer
E. All of the answers are correct
Q: What factor contributes to the
bent shape of a water molecule?
A. The dipole arrows in a water molecule
B. The unshared electron pairs on the oxygen atom
C. The electronegativity differ- ence between hydrogen and oxy- gen
D. The unequal electron sharing between hydrogen and oxygen E. None of the answers
are cor- rect
Answer
B. The unshared electron pairs on the oxygen atom
Q: The H+ concentration of a solu- tion is 5.6 x 10^-5. What is the pH?
A. -4.25
B. 4.25
C. 5.65
D. -9.75
Answer
E. 9.75
B. 4.25
[H+] = 5.6 x 10^-5
pH = -log[5.6 x 10^-5] = 4.25
Q: The H+ concentration of a solution is 1.2 x 10^-3 M. What is the pH?
CHEM210 / CHEM 210 Module 1: (Latest Update
2026 / 2027) Organic Chemistry | Questions &
Answers | Grade A | 100% Correct – Portage
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Q: T/F according to the module, a compound with a molecular mass of 3,000 g/mol is
considered a macromolecule
Answer
false
Q: T/F biomolecules can have only two functional groups
Answer
false
Q: T/F in a eukaryotic cell, the organelles called peroxisomes serve the purpose of
digesting macromolecules
Answer
false
Q: T/F carbon dioxide has a linear molecular shape AND has a bond angle of 120
Answer
false
Q: of the following, ______ is not a property of carbon
A. forming ionic bonds
B. forming cyclic structures
C. forming multiple bonds
D. forming bonds with oxygen
E. forming in long chains
Answer
A. forming ionic bonds
Q: Which of the following is an element not typically found in living organisms?
A. Br
B. Ca
C. H
D. S
E. Na
Answer
A. Br
Q: ______ is a functional group found in carbohydrates
A. esters
B. thiols
C. carboxylic acids
D. alcohols
E. amines
Answer
D. alcohols
Q: A ________ is a chemical formula that does not show the C-H and C-C bonds
A. covalent formula
B. line bond formula
C. empirical formula
D. Kekule's structure
E. condensed formula
Answer
E. condensed formula
Q: In biomolecular structure, if two macromolecules interact it is called a _______.
A. monomer
B. dimer
C. macrocolecular structure
D. supramolecular complex
E. quasimer complex
Answer
D. supramolecular complex
Q: an organic compound with this structure, C=C, contains a ______ functional
group
A. alkane
B. alkene
C. alkyne
D. alcohol
E. both b and d
Answer
B. alkene
Q: scientists refer to ________ as the "super glue" of the chemistry
A. C
B. Co
C. Na
D. N
E. O
Answer
A. C
Q: what energy molecule is produced via respiration?
A. ATP
B. Creatine
C. DNA
D. RNA
E. mitochondria
Answer
ATP
Q: what would be the approximate size of a human cell?
A. 0.1 inch
B. 1 nm
C. 10 nm
D. 10 um
E. 10 cm
Answer
D. 10 um
Q: for butane, there are ______ carbon and _____ hydrogen atoms
A. 4, 8
B. 4, 10
C. 8, 4
D. 8, 10
E. both b and d
Answer
B. 4,10
Q: for an organic compound, which structure is the most efficient to draw?
A. condensed
B. Kekule'
C. line bond
D. structural
E. none of these
Answer
C. line bond
Q: when writing an organic functional group, scientists often write an "R" as part of
the structure. what does the R indicate?
A. argon
B. rest of the molecule
C. routine carbon atom
D. a string of carbon atoms
E. none of the above
Answer
B. rest of the molecule
Q: according to the module, the study of non-carbon compounds is referred to as
_______
A. organic chemistry
B. inorganic chemistry
C. biochemistry
D. environmental chemistry
E. none of the above
Answer
B. inorganic chemistry
Q: the _____ functional group was not discussed in this module
A. alcohol
B. amine
C. aromatic
D. thiol
E. all of these were discussed
Answer
E. all of these were discussed
Q: which number would be closest to the approximate number of ribosomes in an E.
coli cell?
A. 1
B. 25
C. 250
D. 25,000
E. both c and d
Answer
D. 25,000
Q: which of the following would most likely have a cell wall?
A. marigold flower cells
B. deer cells
C. heart cells
D. human red blood cells
E. all of the above
Answer
A. marigold flower cells
Q: eukaryotes have molecules that provide a protective structure. this network, which
is found in all eukaryotes, is called the ________
A. cell wall
B. cytoskeleton
C. cytosol
D. cytoplasm
E. none of the above
Answer
B. cytoskeleton
Q: the molecule linked to the medical condition of gout is ______
A. uric acid
B. luciferin
C. liciferase
D. glucose
E. glycine
Answer
A. uric acid
Q: about how many different elements are found in living organisms?
A. 9
B. 30
C. 50
D. 68
E. 92
Answer
B. 30
Q: T/F according to the module, a compounds with a molecular mass of 8,000 g/mol
is considered a macromolecule
Answer
true
Q: T/F biomolecules can have two or more different functional groups
Answer
true
Q: T/F carbon dioxide has a linear molecular shape AND has a bond angle of 180
Answer
true
Q: of the following, ________ is not a property of carbon
A. forming covalent bonds
B. triple bond formation
C. possessing five valence electrons
D. reacting to form long chains called polymers
E. forming multiple bonds
Answer
C. possessing five valence elections
Q: which of the following is an element not typically found in living organisms?
A. Se
B. S
C. P
D. F
E. Na
Answer
D. F
Q: A ______ is a chemical formula that shows how the atoms of a molecule are
bonded to one another
A. structural formula
B. line bond formula
C. empirical formula
D. ionic formula
E. condensed formula
Answer
A. structural formula
Q: a collection of two or more macromolecules uniting is called a _______
A. supramolecular complex
B. monomer
C. macromolecular structure
D. dimer
E. Kekule' complex
Answer
A. supramolecular complex
for propane, there are ______ carbon and ______ hydrogen atoms
A. 5, 12
B. 4, 10
C. 3, 6
D. 3, 5
E. none of the above
Answer
E. none of the above
which of the following would most likely have a cell wall?
A. monkey cells
B. snake cells
C. red algae cells
D. human red blood cells
E. all of the above
Answer
C. red algae cells
T/F according to the module, a compound with a molecular mass of 1,000 g/mol is
considered a macromolecule
Answer
false
T/F carbon dioxide has a linear molecular shape AND has a bond angle of 109.5
Answer
false
what molecule is the most important for energy storage in cells?
A. creatine
B. mitochondria
C. DNA
D. RNA
E. ATP
Answer
E. ATP
what would be the approximate size of a human cell?
A. 12 um
B. 1 nm
C. 15 nm
D. 0.2 inch
E. 15 cm
Answer
A. 12 um
for pentane, there are _____ carbon and ______ hydrogen atoms
Answer
5, 12
according to the module, the study of carbon compounds is referred to as _______
A. organic chemistry
B. inorganic chemistry
C. biochemistry
D. environmental chemistry
E. none of the above
Answer
A. organic chemistry
which number would be closest to the approximate number of ribosomes in an E. coli
cell?
A. 9
B. 38
C. 400
D. 1,500
E. 26,000
Answer
E. 26,000
for propane, there are ______ carbon and ______ hydrogen atoms
A. 5, 12
B. 4, 10
C. 3, 8
D. 3, 5
E. none of the above
Answer
C. 3, 8
H2O makes up _____% of more of living things
Answer
70%
some plant species are _____% water by mass
Answer
90%
T/F in a eukaryotic cell, the organelle called a lysosome serves the purpose of digesting
macromolecules
Answer
true
T/F carbon dioxide has a tetrahedral molecular shape AND has a bond angle of 180
Answer
false
which of the following is an element not typically found in living organisms?
A. N
B. He
C. H
D. S
E. O
Answer
B. He
which of the following would most likely have a cell wall?
A. human brain cells
B. fungal cells
C. snake cells
D. muscle cells
E. all of the above
Answer
B. fungal cells
T/F in a eukaryotic cell, the organelle called ribosomes serve the purpose of digesting
macromolecules
Answer
false
an organic compound with this structure, C-OH, contains a _____ functional group
A. alkane
B. alkene
C. alkyne
D. alcohol
E. both b and d
D. alcohol
T/F biomolecules can have only one functional group
false
What are three ways that biochemists study biological organisms?
Biochemists study 1) the relationship between structure and function of biomolecules, 2)
chemical reactions of organisms (metabolism), and 3) communication within and
among organisms.
What is the definition of biochemistry?
Often referred to as the chemistry of life, biochemistry asks how the remarkable
properties of organisms relate to their molecules.
What is another name for firefly?
lightning bug
Is Li an element common in biological organisms?
No. See Figure 1.3 for the common elements.
What is known as the "medium of life"?
Water
What is the bond angle associated with trigonal pyramidal shape?
107.5 degrees
Are transition metals commonly found in biological organisms?
Yes. They are trace elements in organisms. See Figure 1.3 for examples.
True or false: Water can make up 85% (by mass) of a living organism.
True. Some plants are made up of 90% water by mass.
True or false: Large elements tend to make the strongest covalent bonds.
False. Smaller elements tend to make the strongest bonds due to significant overlap.
Name three bulk elements. Name three trace elements.
Bulk elements: H, C, N, O, Na, P, S, Cl, K, and Ca, Trace elements: Mg, V, Cr, Mn, Fe,
Co, Ni, Cu, Zn, Se, Mo, I, and W.
Differentiate between inorganic chemistry and organic chemistry.
Organic chemistry is the study of carbon-based compounds. Inorganic chemistry is the
study of all other elements.
Is H2O an organic molecule? How about CO2? C100H202?
Water is not organic; it does not contain carbon. Both CO2 and C100H202 are organic
compounds.
The next row of Table 1 would be the 6-carbon alkane, hexane. Write out its chemical
formula and condensed formula.
chemical formula: C6H14, Condensed formula: CH3CH2CH2CH2CH2CH3
On your own paper, draw the Kekule structures and line-bond formulas for both butane
and hexane. When you have drawn the structures, enter a note in the answer box
indicating you have done so (e.g., "I completed these drawings." Or "I drew the
structures for butane and hexane.")
How are the aldehyde and ketone functional groups similar? Different?
Aldehdyes and ketones both have a carbon double bond oxygen arrangement (C=O) in
their structure. They differ in that the other two bonds that the carbon forms are
different. A ketone has both bonds connected to other carbons. An aldehyde has one
bond to hydrogen and the second bond to either another hydrogen or carbon.
What functional groups are found in glycine?
Carboxylic acid and amine
Retinal is found in the retina and helps with the absorption of light. What are two
functional groups found in Retinal?
alkene and aldehyde
A cell wall is a combination of carbohydrates and proteins. What level of organization
would this indicate and why?
Supramolecular complex. A cell wall is a combination of two types of macromolecules to
form a larger complex (through non-covalent interactions).
What is the monomer of proteins, carbohydrates, and DNA?
The protein monomer is an amino acid, a monosaccharide is the monomer for
carbohydrates, and a nucleotide is the monomer for DNA.
How are prokaryotes and eukaryotes different? (State your answer in two or more
complete sentences.)
While they are both cells types, prokaryotes have a simple structure with no organelles
present. Eukaryotes have a true nucleus and organelle structures. As a result, the
eukaryotes are also considerably larger than prokaryotes.
How are Bacteria and Archaea different? (State your answer in two or more complete
sentences.)
Bacteria and Achaea are both simple cells with no organelle structure, and they lack a
true nucleus. Archaea live in extreme conditions, such as hot springs and in the artic;
they are thought to be more closely related to prokaryotes.
What is the function of mitochondria, lysosomes, and vacuoles?
The mitochondria is the powerhouse of the cell responsible for producing ATP. It also
contains metabolic processes that yield ATP in the end. - Lysosomes degrade
macromolecules-protein, lipid, carbohydrate, nucleic acids-into smaller pieces. These
organelles have an acidic pH. Vacuoles have digestive enzymes to degrade proteins,
carbohydrates, and nucleic acids, plus vacuoles function largely as storage centers.
What energy molecule is produced in the mitochondria?
Adenosine triphosphate (ATP)
CHEM210 / CHEM 210 Final Exam | Latest
2026–2027 Update | Organic Chemistry |
Portage Learning | Verified Questions &
Answers | Grade A
Q: Wh
...
at is ground state electron configuration of Co?
[Ar]3d^9
[Ar]4s^1 3d^8
[Ar]4s^2 3d^7
[Ar]4s^2 4p^6 4d^1
Answer
[Ar]4s^2 3d^7
Q: molybdenum has an anomalous electron configuration. using the shorthand
notation for electron configurations, write the electron configuration
A) [kr]5s 4d^6
B) [kr]5s 4d^0 5p^6
C) [kr]5s^1 4d^5
D) [kr]5s^2 4d^4
Answer
C) [kr]5s^1 4d^5
Q: the symbol [Kr] represents
a) 4s^2 4p^6
b) 1s^2 2s^2 2p^6 3s^6 4s^2 4p^6
c) 1s^2 2s^2 2p^6 3s^6 4s^2 3d^10 4p^6
D)1s^2 2s^2 2p^6 3s^6 4s^2 3d^10 4p^6 4d^10
Answer
c) 1s^2 2s^2 2p^6 3s^6 4s^2 3d^10 4p^6
Q: What is the wavelength of UV light in the balmer series when m=2 and n=7?
a) 0.00252 nm
b) 397 nm
c)337 nm
d)0.00297 nm
Answer
b) 397 nm
Q: How many electrons can a single orbital hold?
A) 2n
B) 2
C) 2l+1
D)8
Answer
B) 2
Q: What are the possible values of I and m1 for an electron in a 5d orbitial?
A) I=0 and mI=0
B) I=3 and MI=-2,-1,0,+1, or +2
c) I=1 and MI=-1,0,+1
D) I=2 and MI=-2,-1,0,+1, +2
Answer
D) I=2 and MI=-2,-1,0,+1, +2
Q: What is the the de Broglie wavelength of an electron (m=9.11e-31 kg) moving at a
velocity of 3.0e7m/s?
a) 3.9e-12
b)2.4e-11
c)3.3e-8
d)1.1e-4
Answer
b)2.4e-11
Q: What is the frequency of a helium-neon laser light with a wave of 632.8 nm?
a) 4.47e14 s-1
b)4.47e5 s-1
c)2.11e-15 s-1
d)1.58e-15 s-1
Answer
a) 4.47e14 s-1
Q: What is the correct nuclear symbol for the unknown product "X" in the nucl
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