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WGU C785 Biochemistry – Western Governors University – Academic Year 2026 – Complete Exam Questions with Verified Answers

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This document contains a comprehensive collection of exam questions and verified answers for the WGU C785 Biochemistry course, tailored for the 2026 academic year. It covers essential biochemistry concepts including amino acid structure, enzyme function, protein folding, gene expression, metabolic pathways, and molecular biology processes such as transcription, translation, and DNA replication. Ideal for exam preparation, this guide is structured in a Q&A format for efficient revision and covers all major topics relevant to the C785 exam. Keywords: biochemistry exam prep amino acid structure enzyme inhibition protein folding DNA replication RNA transcription gene expression metabolic pathways glycolysis citric acid cycle electron transport chain hemoglobin vs myoglobin fatty acid metabolism gluconeogenesis PCR steps mutation types MCADD essential fatty acids insulin and glucagon pathways ATP synthesis

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WGU C785 BIOCHEMISTRY 2026 EXAM
QUESTIONS AND ANSWERS | 100%
PASS



What is the basic structure of an amino acid? What do they look like? -

🧠ANSWER ✔✔amino group (NH2 or NH3), carboxyl group (COO or

COOH), alpha carbon (C), and variable group

How do you identify the 3 different types of side chains: non-

polar/hydrophobic, polar, and charged? - 🧠ANSWER ✔✔Non-

polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH,

SH, or NH. Charged - end with a charge

,what kinds of bonds do each of the 3 different types of side chains make? -

🧠ANSWER ✔✔ionic, hydrophobic/non-polar, charged


What are the 4 levels of protein structure? - 🧠ANSWER ✔✔Primary - linear

structure, Secondary - Folded into helix or pleated sheet caused by

hydrogen bonding, tertiary - 3D structure caused by side chain interactions,

quaternary - 1+ amino acid chains combine = multiple subunits MUST have

1+ subunit

What enviormental change breaks each type of bond? - 🧠ANSWER

✔✔hydrophobic - temperature change, ionic - salt or decreased pH,

hydrogen - temperature, change in pH, disulfide - reducing agents

what type of amino acid side chain leads to protein aggregration? -

🧠ANSWER ✔✔hydrophobic bonds


how do environmental changes affect protein folding? - 🧠ANSWER

✔✔Extreme temp can cause hydrogen bonds to break apart =

malformation of protein folding


how do mutations affect protein structure? - 🧠ANSWER ✔✔Can cause

structure to change. Protein loses form = loses function. May form a

different protein.

,What is an electron? - 🧠ANSWER ✔✔Negatively charged atom on outer

ring for bonding


What is energy: - 🧠ANSWER ✔✔Power derived fro chemical interaction


what are covalent bonds? - 🧠ANSWER ✔✔chemical bond, atoms share 1+

valence electrons


what is an ionic bond? - 🧠ANSWER ✔✔bond between positive and

negative


what is a hydrogen bond? - 🧠ANSWER ✔✔weak bond between positive

and negative


with an amino? - 🧠ANSWER ✔✔piece of amino acid, NH2 or NH3


what is a carboyxl? - 🧠ANSWER ✔✔piece of amino acid, COO or COOH


What is hydrophobic? - 🧠ANSWER ✔✔Doesn't like water, end with CH


what is hydrophilic? - 🧠ANSWER ✔✔Water Lovering, end with OH, NH, or

SH


what is disulfide bond? - 🧠ANSWER ✔✔strongest bond between reduction

agents, formed between SH's.


3
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, what are zwitterions? - 🧠ANSWER ✔✔amino with positive and negative

charges = overall charge of zero


what is a polypeptide - 🧠ANSWER ✔✔polymer of amino acids


What is dehydration synthesis? - 🧠ANSWER ✔✔Process of forming peptide

bonds


what is hydrolysis? - 🧠ANSWER ✔✔adding water to destroy bonds


what is an alpha helix? - 🧠ANSWER ✔✔twisted secondary structure,

formed by hydrogen bonds


what is a beta sheet? - 🧠ANSWER ✔✔folded second structure shape,

formed by hydrogen bonds


what is denaturation? - 🧠ANSWER ✔✔loss of shape duet o interruption of

chemical bonds; occurs via extreme salt, temp, pH


what is aggregation? - 🧠ANSWER ✔✔clumping of inner or outer cellular

proteins caused by misfolded proteins leading to diseases such as

Alzheimers, ALS, Parkinson's


how do enzymes catalyze reactions? - 🧠ANSWER ✔✔bind with substrates

to decrease activation energy required and decrease reaction rate

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