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BIOL 200 Midterm Exam Questions (85) Protein Structure Membranes Transcription UBC 2026

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This document contains approximately 85 carefully structured exam questions and verified answers for BIOL 200, focusing on key midterm topics such as protein structure (primary to quaternary), peptide bonding, membrane biology, lipid bilayers, transcription mechanisms, RNA processing, chromatin organization, and cellular transport systems. The content is presented in a concise question-and-answer format that supports active recall and rapid revision, making it highly effective for exam preparation. The material closely aligns with core concepts taught in undergraduate molecular biology and cell biology courses, with strong parallels to widely used textbooks such as Molecular Biology of the Cell by Bruce Alberts and Lehninger Principles of Biochemistry by Nelson and Cox. It integrates both conceptual understanding and mechanistic detail, including processes like transcription initiation, RNA splicing, membrane fluidity, and protein folding interactions. This resource is particularly suitable for students enrolled in BIOL 200 at the University of British Columbia (UBC), as well as similar introductory courses in molecular biology, biochemistry, and cell biology at other institutions. It is ideal for undergraduate students in biology, biomedical sciences, life sciences, and pre-med programs. Additionally, it can benefit students preparing for midterms, cumulative exams, or standardized tests requiring a strong understanding of molecular and cellular processes. The structured format also makes it compatible with flashcard-based study tools such as Anki. Keywords: protein structure, peptide bonds, alpha helix, beta sheet, membrane biology, lipid bilayer, transcription, RNA processing, chromatin, histones, gene expression, enzyme activity, molecular biology, cell biology, biochemistry exam, UBC biology, anki flashcards

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BIOL 200 UBC
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BIOL 200 UBC Midterm 2026
Exam Questions and Verified
Answers | Already Graded A+



What bonds form in a primary protein structure? - 🧠 ANSWER ✔✔covalent

bonds between the backbone, peptide bonds


What bonds form in a secondary protein structure? - 🧠 ANSWER ✔✔non

covalent bonds between backbone

,What bonds form in a tertiary protein structure? - 🧠 ANSWER ✔✔covalent

bonds between R groups (i.e. disulfide), non-covalent bonds between

backbone, R groups


What bonds form in a quaternary protein structure? - 🧠 ANSWER ✔✔-

covalent bonds between R groups (i.e. disulfide), non-covalent bonds

between backbone, R groups

-between 2+ polypeptides


How is a peptide bond formed? - 🧠 ANSWER ✔✔condensation reaction

between alpha amino group of one amino acid and carboxyl group of

another

Why are some folding patterns not obtainable by primary structures? - 🧠

ANSWER ✔✔resonance between C-O and C-N constrains flexibility, no

free rotation around C-N axis


What bonds stabilize primary structures? - 🧠 ANSWER ✔✔peptide bonds


What bonds stabilize secondary structures? - 🧠 ANSWER ✔✔H-bonds

between N-H, C=O groups

, What types of structures result from secondary protein folding? - 🧠

ANSWER ✔✔alpha helix, beta sheet


Describe the bonds of an alpha helix. - 🧠 ANSWER ✔✔carbonyl forms H-

bond with H from N-H of a residue, 4 residues further on sequence (in

same chain), side chains point outward


Describe the bonds of a beta sheet. - 🧠 ANSWER ✔✔polypeptide folds

back on itself, H-bonds form between N-H and C=O on neighbouring

polypeptide strands, side chains project upwards & downwards

What factors determine which structure forms in secondary folding? - 🧠

ANSWER ✔✔interactions between side chains of amino acid residues in

polypeptide such as: steric hinderance, charge repulsion, proline presence,

presence of other chem groups


What bonds stabilize tertiary structures? - 🧠 ANSWER ✔✔ionic bonds

between side chains, H-bonds, LDF (weaker so need more to stabilize),

covalent disulfide bond between cysteine

How does hydrophobic interactions take part in tertiary formation? - 🧠

ANSWER ✔✔most stable when hydrophobic residues face inwards,

surrounded by other parts of the protein

3
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