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WGU BIOCHEMISTRY PRACTICE TEST PAPER 2026 FULL QUESTIONS AND ANSWERS

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WGU BIOCHEMISTRY PRACTICE TEST PAPER 2026 FULL QUESTIONS AND ANSWERS

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Subido en
23 de noviembre de 2025
Número de páginas
19
Escrito en
2025/2026
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Examen
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WGU BIOCHEMISTRY PRACTICE TEST PAPER
2026 FULL QUESTIONS AND ANSWERS

◉ A point mutation in which a single nucleotide change results in a
codon that codes for a DIFFERENT amino acid. Answer: What is a
Missense Mutation?


◉ It is typically not seen in every generation of an affected family. X-
linked dominant disorders are caused by mutations in genes on the
X chromosome, one of the two sex chromosomes in each cell. (males
and females are equally affected) Answer: What is Autosomal
Dominate?


◉ It becomes Ionized Alanine. (Alanine is HYDROPHOBIC and has
CH3 as its weak interaction. Ionized means it has a + or -. Answer:
Alanine is an amino acid with an amino group, a carboxyl group, and
a methyl group (side chain). What happens if it looses an electron.


◉ Amino Acids whose side chains prefer water. (NH, OH, SH)
Answer: What is a Polar Amino Acid?


◉ Amino Acids that Can't Have (CH) water (hydrophobic) Answer:
What is a Non Polar Amino Acid?

,◉ There is a charge (+/-) attached to the amino acid Answer: What
is Ionized Amino Acid?


◉ It is caused by tangles inside the cell and plaques outside the cell
(senile plaques) caused by abnormal protein aggregation (APA).
Answer: What is the misfolding of protein structure in Alzhiemers
disease?


◉ It is a fibrous, toxic material inside of cells. When its connections
are lost, it becomes defective and forms filaments in the neuron. Its
accumulation is triggered by a buildup of Amyloid protein, which
disrupts the functioning of brain cells. Answer: What roll does the
protein TAU play in Alzhiemers disease?


◉ It is a buildup of excess Amyloid protein between nerve cells. It
starts in the hippocampus and moves up, creating senile plaques in
the brain. Answer: How is Amyloid-beta protein linked to
Alzhiemers Disease?


◉ Protein aggregates usually consist of fibers containing misfolded
protein with a β-sheet conformation, termed amyloid.
Neurodegenerative diseases such as Alzheimer's disease (AD),
Parkinson's disease (PD), Huntington's disease (HD), amyotrophic
lateral sclerosis (ALS) and prion diseases have these protein
aggregations. Neurodegeneration and memory loss can be detected
before Amyloid fibers accumulate in the brain. Answer: What is
Neurodegenerative protein aggregation?

, ◉ Proteins that bind to denatured proteins and assist in the PROPER
folding or unfolding and the assembly or disassembly of molecular
structures. (they can help newly formed proteins and help misfolded
proteins) Answer: What is a molecular chaperone?


◉ Primary, (formed by peptid bonds)
Secondary, (held together by hydrogen bonds, formed from two
polar amino acids)
Tertiary, (side chain interaction)
Quaternary (more than one polypeptide) Answer: What are the
levels of a protein structure?


◉ The folding and intramolecular bonding of the linear amino acid
chain. Folded proteins are stabilized by thousands of noncovalent
bonds between amino acids. THE AMINO ACID SEQUENCE OF A
PROTEIN DETERMINES ITS 3D SHAPE. Answer: What determines
the 3D shape of a protein?


◉ Folded structures that form within a polypeptide. Stabilized by
HYDROGEN BONDS between atoms in the polypeptide backbone.
How the chains on amino acids interact with each other to form
BETA SHEETS and ALPHA HELIXES. Answer: What is the Secondary
level of protein structure?
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