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CHEM 210 Module 3 Exam - Biochemistry Proteins, Enzymes, Amino Acids Q&A 2025, Exams of Nursing

Liberty University (LU)Nursing

CHEM 210 Module 3 exam review on biochemistry. Covers protein functions, amino acid groups, enzyme inhibition, peptide bonds, cofactors, and enzyme classes. Essential study resource. biochemistry exam, study guide, college biology, CHEM 210, module 3, protein structure, enzyme function, amino acids, peptide bonds, cofactors, enzyme inhibition, university test, science students

Typology: Exams

2024/2025

Available from 08/31/2025

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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 - Biochemistry Proteins, Enzymes, Amino Acids Q&A 2025 and more Exams Nursing 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 andcarboxylic 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 the amine 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. 10. Proteins typically adopt either a conformation that is fibrous or

is anadvantage (and disadvantage) in protein structure.

  1. 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 twenty amino acids ANS oligopeptide
  1. coiled structures of amino acids where the backbone atoms form hydrogen bonds 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 to another compound. ANS substrate
  4. the enzyme, acts to break the double bond of the substrate by adding water across the double bond ANS fumarase
  5. which is a class of enzymes that creates double bonds or adds molecules to double bonds. ANS lyases
  6. catalyze oxidation and reduction reactions ANS Oxidoreductases
  7. catalyze the transfer of a group from one molecule to a second ANS transferals
  1. catalyze the breaking, or hydrolysis, of bonds ANS hydrolases
  2. catalyze the forming or breaking of double bonds ANS lyases
  3. catalyze the rearrangement within a single molecule ANS isomerases
  4. catalyzes the joining of two molecules, or two parts of a molecule ANS ligases
  5. Some enzymes, including fumarase, have non-protein components ANS cofac-tors

52. can bind either to the lone enzyme or the enzyme-substrate complex. ANS - 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 often referred 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 polypeptide chains 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 the amino 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 with the release of water
  8. how does a dipeptide continue to grow ANS amino acids added to carboxy end
  1. term used to describe the chemistry of large compounds ANS supramolecularchemistry