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CHEM 210 Final Exam Bundle (Exams 1–8) with Verified Answers – Complete Study Guide 2025, Exams of Nursing

Rasmussen College - FloridaNursing

CHEM 210 complete final exam bundle covering Exams 1 through 8 with 234+ verified questions and answers. Topics include biomolecules, organic functional groups, amino acids, enzymes, nucleic acids, carbohydrates, lipids, citric acid cycle, glycolysis, beta-oxidation, urea cycle, and oxidative phosphorylation. A comprehensive exam prep guide for chemistry and biochemistry students. chem 210 final exam bundle, chemistry exam pack, biochemistry final exam prep, glycolysis and citric acid cycle questions, amino acids chemistry test, nucleic acids exam study guide, organic chemistry practice exam, enzymes and proteins test bank, lipids and carbohydrates exam prep, oxidative phosphorylation exam

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CHEM 210 Exam 1 - 8
Questions and Answers (Verified Answers)
1. According to the Module, a compound with a molecular mass of 8,000 g/mol
is considered a macromolecule.: True
2. Biomolecules can have only two functional groups.: False
3. The following functional group is an amine.: True
4. In a eukaryotic cell, the organelles called ribosomes serve the purpose of
digesting macromolecules.: False
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Download CHEM 210 Final Exam Bundle (Exams 1–8) with Verified Answers – Complete Study Guide 2025 and more Exams Nursing in PDF only on Docsity!

C HEM 210 Exam 1 - 8

Questions and Answers (Verified Answers)

  1. According to the Module, a compound with a molecular mass of 8,000 g/mol is considered a macromolecule.: True
  2. Biomolecules can have only two functional groups.: False
  3. The following functional group is an amine.: True
  4. In a eukaryotic cell, the organelles called ribosomes serve the purpose of digesting macromolecules.: False
  1. Carbon dioxide has a linear molecular shape AND has a bond angle of 180o: True
  2. Of the following, is not a property of carbon.: possessing five valence electrons
  3. Which of the following is an element not typically found in living organ- isms?: Br
  4. Which of the following functional groups is prominent in carbohydrates?: - Alcohols
  5. The following functional group is an example of .: Ketone
  6. A is a chemical formula that shows how the atoms of a
  1. For an organic compound, which structure is the most efficient to draw?- : Line bond
  2. When writing an organic functional group, scientists often write an "R" as part of the structure. What does the R indicate?: Rest of the molecule
  3. According to the module, the study of NON-carbon compounds is referred to as .: Inorganic chemistry
  1. Which of the following is not a functional group discussed in this module?- : All of these were discussed.
  2. Which number would be closest to the approximate number of ribosomes in an E. coli cell?: 25,
  3. Which of the following would most likely have a cell wall?: Fungal cells
  4. Eukaryotes have molecules that provide a protective structure. This net- work, which is found in all eukaryotes, is called the .: Cytoskele- ton
  5. What is the molecule responsible for gout?: Uric acid
  6. About how many different elements are found in living organisms?: 30

other elements (N and O). 3. Carbon can form long chains by forming numerous carbon-carbon bonds; we call these large molecules polymer. 4. Lastly, carbon can form cyclic structures, which are also called ring compounds.

  1. What the definition of inorganic chemistry? How does it differ from organic chemistry?: Inorganic chemistry is the study of all other elements, but carbon. Organic chemistry is the study of carbon-based compounds both in living and non-living organisms. There is no need to have separate sub-disciples for organic and inorganic chemistry, but for historical and organizational reasons, the difference exists.
  2. Biochemists study the communication within and among organisms. Ac- cording to the module, what are two other aspects of living organisms that

biochemists study?: In the module, biochemists also study the structure and function of biomolecules and the chemical reactions of organisms.

  1. The pH of a solution of 3.2 x 10 - 10 M NaOH is:: 4.5 ([Kw=[H+][OH-] = 1.0 x 10 - 14; [H+][3.2 x 10-10] = 1.0 x 10-14 ;[H+]=3.1 x 10-5; pH=-log[3.1 x 10-5]=4.5])
  2. Which attribute contributes to water's unusual properties?: All of the an- swers are correct
  3. The bent shape of water is due to .: The unshared electron pairs on the oxygen atom
  4. Which diagrams correctly represent a hydrogen bond?: A and D both show a proton donor and acceptor
  1. Which of the following is the change in entropy of a reaction?: None of the above
  1. Which buffer system is used by the blood to maintain pH balance?: Bicar- bonate buffer system
  2. A buffer can neutralize only a certain amount of acid and base. We say that this is its: Buffer capacity
  3. Is a pH of 7.00 acidic, neutral, or basic?: Neutral
  4. The "ion product" is equal to what value?: 1.0 x 10 - 14
  5. In equilibrium constant expressions, the concentration is expressed in units of as indicated by the brackets [ ].: molarity
  6. A pH = 5.0 indicates a concentration of OH- (in M) of : 10 - 9
  7. Which of the following compounds would not be soluble in water?: Oil
  8. The hybridization of the central atom in water is .: sp
  9. Four identical molecules dissolve in water. Each molecule contains both a polar portion and nonpolar portion of structure. The four molecules interact in such a way that the nonpolar sections align. This is an example of the .: Hydrophobic effect
  10. How does the strength of a hydrogen bond compare to the strength of a London Force? Also, how about the strength of a hydrogen bond compared to a dipole-dipole force? Briefly comment on these differences.: The hydrogen bond strength is between 12 and 16 kcal, while the London force is generally less

C) "+"

D) entropy E) "+"

  1. What is the hydrophobic effect and how does a clathrate help explain this phenomenon?: The hydrophobic effect helps scientists explain how biological molecules form and interact. For instance, when molecules with both a nonpolar and polar regions dissolve in water, the nonpolar regions pack together. The packing of the nonpolar regions minimizes the interaction with water and the polar region interact with water, which in total is called the hydrophobic effect. The driving force behind this effect is the spontaneous drive of water to bind to itself through hydrogen bonds. To maximize the hydrogen bonds, water orders itself around the hydrophobic portion of the nonpolar regions in a cage structure also called a clathrate. In so doing, water can form bonds with itself and also permit the nonpolar regions to be dissolved.
  2. he amino acids serine and threonine both contain sulfur atoms.: False
  3. The following secondary structure shown below is an example of an alpha helix.: True
  4. The side chain of histidine is bonded to the backbone nitrogen atom: False
  5. The name of the molecule that binds to an enzyme is called the holoen-

zyme.: False

  1. An inhibitor that binds at the active site is a coenzyme.: False
  2. Which amino acids differ by only one atom?: Ser and Cys
  3. The formation of a peptide bond between two amino acids is an example of a(n) reaction.: Condensation
  4. The peptide Ala-Glu-Gly-Ala has .: Three peptide bonds
  5. Formally, when there are 100 or more amino acids are covalently linked together that is called a .: Protein
  6. What unit is used by biochemists to indicate the mass of a protein?: Da
  7. All of the 20 standard amino acids contain an R-group that is attached to the: A. Carboxyl group B. Amino group C. ±carbon D. ²carbon E. It depends on the amino acid: C
  8. Which of the following correctly matches the amino acid with its one letter abbreviation?: Aspartic acid, D
  9. The order of amino acids in a protein is written .: N to C-terminus
  1. In an alpha helix, the R groups on the amino acid residues:: Are found on the outside of the helix spiral
  2. Motifs are classified primarily by their:: Content and arrangement of the secondary structure
  3. The secondary structure shown below is an example of a(n):: Parallel beta sheet
  4. A single folded polypeptide has a globular shape, which describes its structure.: Tertiary
  5. How many classes of enzymes are recognized by the IUBMB?: 6
  6. An enzyme requires Cr+3 for catalysis. Under conditions of chromium deficiency, when the enzyme lacks chromium, this enzyme would be referred to as a(n):: Apoenzyme
  7. When a substrate has just started its conversion to a new molecule, it is said to be in the .: Transition state
  8. What three factors influence the rate of an enzyme-catalyzed reaction?: - pH, concentration, and temperature
  9. Which of the following describes induced fit?: Substrate binding induces a conformation change in the enzyme
  10. The ES stands for:: Enzyme-substrate

ing protein. e.: There are ay be present,

  1. Any molecule or ion that is necessary for an enzyme's function is called a:: Cofactor
  2. Identify the types of secondary structure present in the follow Also, determine the numbers of each type of secondary structur one alpha helix and two beta strands (or one beta sheet). Beta turns m but are not required in the answer.
  3. Hemoglobin is said to be a tetramer. A) What is a tetramer? B) Structurally, a tetramer describes what level of protein organization?: A) Simply it means that hemoglobin has four subunits or four independent polypeptide chains interacting non-covalently. Each protein molecule is composed of two copies each of two different subunits a and b. We say that hemoglobin is a tetramer because it has four polypeptide chains. B) It is describing the quaternary structure, which has two or more independent

structure, including the connections between them. Motifs are found in a variety of proteins from across all organisms.

  1. What would "PRSGED" indicate about the structure and composition to a protein scientist? Explain in at least two complete sentences.: The "PRSGED" is an example of protein primary structure, which is the order of amino acids in a peptide or protein. Each of the letters (i.e. P, R, ...) represents one of the 20 amino acids as a one-letter abbreviation). The order of amino acids is written from N-terminal to C-terminal. The letters in this peptide stand for Proline, Arginine, Serine, Glycine, Glutamic Acid, and Aspartic Acid.
  2. What is the spot on an enzyme where reactions take place? Explain the characteristics of this spot.: The active site is the spot on 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.
  3. Which of the following monosaccharides is not an aldose?: Dihydroxyace- tone
  4. When two monosaccharides are epimers:: They differ only in the configura- tion about one carbon atom
  5. Which pair is anomeric?

A) D-ribose and D-galactoseB) ±D- - allose and ²-D-alloseC) D-Ribose and L-fruc- toseD) D-glucose and L-glucoseE) ±D- - idose and ²-L-idose: ±D- - allose and ²-D-al- lose

  1. When forming the disaccharide maltose from two glucose monosaccha- rides:: A condensation reaction occurs
  2. Amylose and amylopectin are both polymers of: A) ±D- - glucoseB) ²-D-glucoseC) GalactoseD) IdoseE) Maltose: ±D- - glucose
  3. Which statement about starch and glycogen is false? A) Both have ²-D-glucose monomersB) Both starch and glycogen are energy storage polysaccharidesC) Both are homopolymers of glucoseD) Glycogen is more extensively branched than starchE) Both have O-glycosidic linkages: - Both have ²-D-glucose monomers
  4. Which monosaccharide is not a six-carbon monosaccharide?: Dihydroxy- acetone
  5. The two monosaccharides shown below could best be described as:: - Epimers