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CHEM 210 Module 3 Exam – (2026) Actual Questions & Answers (Biochemistry) 100% Guarantee, Exams of Biochemistry

Liberty University (LU)Biochemistry

CHEM 210 Module 3 Exam includes actual 2026 biochemistry exam questions with verified answers covering protein functions, enzymes, proteases, hormones, amino acids, amine groups, carboxylic acids, protein structure, catalysis, and biological molecules. An ideal study guide for quizzes, module exams, and final exam preparation. CHEM 210 Module 3 Exam, CHEM 210 Module 3 Questions, CHEM 210 Module 3 Answers, CHEM 210 Biochemistry Module 3, CHEM 210 Practice Test, CHEM 210 Study Guide, CHEM 210 Quiz Answers, CHEM 210 Test Bank, CHEM 210 PDF, CHEM 210 Verified Answers, Protein Functions Exam, Protein Structure Questions, Enzyme Questions, Protease Questions, Hormone Functions, Amino Acid Questions, Amino Acid Functional Groups, Amine Group Questions, Carboxylic Acid Questions, Biological Molecules Exam, Biochemistry Practice Questions, College Chemistry Exam, CHEM 210 Latest Exam, CHEM 210 Review Guide, CHEM 210 Biology Chemistry, Module 3 Biochemistry, Chemistry Module 3 Test,

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CHEM 210 Module 3 Exam Newest
1. Name three different functions of proteins. ANS Transport, hormones, catalysis,
structure, and protection
2. What function does a protease have? ANS catalysis. It degrades proteins.
3. What is the function of hormones? ANS These proteins communicate from one cell to
another
4. What are the functional groups common to all amino acids? ANS amine and
carboxylic acid
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Download CHEM 210 Module 3 Exam – (2026) Actual Questions & Answers (Biochemistry) 100% Guarantee and more Exams Biochemistry in PDF only on Docsity!

CHEM 210 Module 3 Exam Newest

  1. Name three different functions of proteins. ANS Transport, hormones, catalysis, structure, and protection
  2. What function does a protease have? ANS catalysis. It degrades proteins.
  3. What is the function of hormones? ANS These proteins communicate from one cellto another
  4. What are the functional groups common to all amino acids? ANS amine and carboxylic acid
  1. Briefly describe the five major groupings of amino acids. ANS The amino acids are grouped into 1) nonpolar, aliphatic 2) nonpolar and aromatic 3) polar but neutral,
  1. acidic, and 5) basic.
  1. What amino acid can form a disulfide bond? ANS Cysteine
  2. Which amino acid is the only one to have its side chain connected to theamine group? ANS proline 8. Consider the following pentapeptide ETYLVD. Which amino acid is at the N terminal? Which is at the C terminal? ANS E is at theN- terminal, and D is at the C-terminal.
  3. Differentiate between protein tertiary structure and protein quaternary structure. ANS Tertiary structure is the conformation or shape of a single polypeptidechain. Quaternary structure is the orientation of multiple subunits.
  1. unique function of proline ANS -structure of proline is not flexible, which is an advantage (and disadvantage) in protein structure.
  2. non-polar aromatic group properties ANS -side chains of these compounds con-tain a ring of carbons as an aromatic functional group -These groups are not as small as the aliphatic, but they are more rigid.
  1. polar amino acids properties ANS -contain side chains that have a dipole, andmost can hydrogen bond
  • interact strongly with water
  1. two cysteines together form ANS disulfide bonds by their sulfur atoms
  2. dipole bonds common in ANS keratin proteins found in hair cells
  3. Amino acids can be joined together into long chains called ANS polypeptides 22. The reaction to two amino acids to form a dipeptide with a peptide bond ANS - peptide bond formation
  4. used to describe a short chain of amino acids usually from two to twentyamino acids ANS oligopeptide

sheets, and (3) beta turns

  1. coiled structures of amino acids where the backbone atoms form hydrogenbonds to stabilize this sequence. ANS Alpha-helices
  2. proteins that accelerate the speeds of chemical reactions ANS enzymes
  3. are the chemical species that bind to the enzyme and are converted toanother compound. ANS substrate
  4. the enzyme, acts to break the double bond of the substrate by adding wateracross the double bond ANS fumarase
  5. which is a class of enzymes that creates double bonds or adds moleculesto double bonds. ANS lyases
  6. catalyze oxidation and reduction reactions ANS Oxidoreductases
  1. catalyze the transfer of a group from one molecule to a second ANS transferals
  2. catalyze the breaking, or hydrolysis, of bonds ANS hydrolases
  3. catalyze the forming or breaking of double bonds ANS lyases
  4. catalyze the rearrangement within a single molecule ANS isomerases
  5. catalyzes the joining of two molecules, or two parts of a molecule ANS ligases
  6. Some enzymes, including fumarase, have non-protein components ANS cofac-tors

mixed inhibitor

  1. which is a four-residue unit that turns 180o degrees ANS beta turn
  2. Collections of particularly stable groups of secondary structures are oftenreferred to as ANS motif
  3. which is a non-amino acid portion of the molecule necessary for the structure and function of the protein. ANS prosthetic group
  4. describes macromolecules that have two or more independent polypeptidechains that associate with one another. ANS quarternary structure
  5. proteins that contain two polypeptides ANS dimer
  6. one oxygen from the carboxylic acid group and two hydrogens from theamino group are lost as water, which is called ANS condensation reaction
  7. how to form peptide bond ANS -amino functional group of one amino acid reactswith the carboxylic acid functional group of a second. -The result is that the two monomers are joined together, producing a dipeptide withthe release of water
  8. how does a dipeptide continue to grow ANS amino acids added to carboxy end
  9. term used to describe the chemistry of large compounds ANS supramolecular chemistry