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Exam (elaborations)

Exam (elaborations) BIOCHEMISTRY Harper's Illustrated Biochemistry, 28th Edition

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This comprehensive set of quizzes, tests, and practice problems provides an in-depth review of critical topics in biochemistry and analytical chemistry. Areas covered include intermediary metabolism, protein chemistry, enzyme kinetics, thermodynamics, membrane biochemistry, bioenergetics, and core principles of analytical chemistry. Designed to support higher education learning, these materials are excellent for undergraduate and postgraduate students seeking to deepen their conceptual understanding, prepare for examinations, or engage in self-directed study. The questions are structured to challenge critical thinking and analytical skills, aligning with university-level coursework and professional standards in the life sciences.

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BCMB322 Prep questions

PROTEIN CHEMISTRY QUIZ 2




Multiple Choice Questions (MCQs) 5. Which amino acid is achiral?
1. Which type of protein is generally insoluble in an a. Alanine
aqueous environment?
b. Valine
a. Globular proteins
c. Glycine
b. Transport proteins
d. Cysteine
c. Fibrous proteins
d. Enzymes
6. Which form of an amino acid carries both positive and
negative charges at neutral pH?
2. Which law is used to determine the configuration of a. Cationic form
amino acids?
b. Anionic form
a. Beer-Lambert Law
c. Nonionic form
b. CORN Law
d. Zwitterion form
c. Dalton’s Law
d. Avogadro’s Law
7. How many peptide bonds are present in a polypeptide
consisting of 245 amino acids?
3. What is the average molecular weight of an amino acid a. 244
residue in a protein after peptide bond formation?
b. 245
a. 128
c. 246
b. 110
d. 243
c. 18
d. 150
8. Who pioneered the use of computational methods in
biochemistry?
4. What kind of proteins help Antarctic fish to survive in a. Dr. Kwadwo Asamoah Kusi
freezing temperatures?
b. Dr. Margaret Oakley Dayhoff
a. Thermophilic proteins
c. Dr. Francis Crick
b. Antifreeze proteins
d. Dr. James Watson
c. Enzymatic proteins
d. sweet proteins


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, BCMB322 Prep questions

9. Which secondary structure is most common in fibrous 13. What kind of proteins are formed by the
proteins? condensation of amino acids?
a. Alpha helices a. Polysaccharides
b. Beta sheets b. Nucleic acids
c. Random coils c. Peptides
d. Mixed secondary structures d. Lipids


10. What property of tryptophan and tyrosine is utilized 14. The CORN law helps in identifying the configuration
in protein quantification? of which carbon in amino acids?
a. High solubility a. Alpha carbon
b. Fluorescence b. Beta carbon
c. Ultraviolet light absorption c. Gamma carbon
d. Thermal stability d. Delta carbon


11. Which proteins are classified as having a mobile or 15. Which protein structure level involves the folding of
dynamic function? the polypeptide into a functional 3D shape?
a. Fibrous proteins a. Primary
b. Structural proteins b. Secondary
c. Globular proteins c. Tertiary
d. sweet proteins d. Quaternary


12. Which amino acid does not possess a side chain that 16. Which protein class is primarily involved in transport
interacts with water at pH 7? functions within the body?
a. Serine a. Fibrous proteins
b. Alanine b. Enzymes
c. Lysine c. Hormones
d. Aspartic acid d. Globular proteins




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Connected book
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Robert K. Murray, Victor W. Rodwell, David Bender, Kathleen M. Botham, P. Anthony Weil, Peter J. Kennelly Harper\'s Illustrated Biochemistry, 28th Edition
Publisher: 2009 ISBN: 9780071701976 Edition: Unknown

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