Zadanie 2b
Describe how differences among amino acids contribute to the variety of protein shapes.
Interactions stabilizing tertiary structure
Compare hydrogen bonding, ionic attraction, disulfide bridges and hydrophobic interactions in folded proteins.
Tę umiejętność sprawdza 9 zadań wzorowanych na arkuszach IB z lat 2022–2025.
Zadania sprawdzające tę umiejętność: 9 Otwórz w wyszukiwarce z filtrami
Zadanie 4
Which pairing correctly explains how a particular level of protein organisation is maintained? A. Primary structure — ionic attractions between separate subunits B. Secondary structure — disulfide links joining every neighbouring residue C. Quaternary…
Zadanie 2c
List two types of side-chain interaction that stabilize a folded polypeptide.
Zadanie 2d
Explain how a globular protein’s amino-acid sequence is related to its tertiary structure.
- Materiał graficzny
Zadanie 6
Which structural interpretation of this hypothetical protein is correct? A. An intrachain disulfide contributes to tertiary structure, and association of two chains gives quaternary structure B. Every line between successive amino acids is a hydrogen bond C.…
- Materiał graficzny
Zadanie 28
A single polypeptide with the ribbon arrangement shown forms a functional enzyme without other polypeptide subunits. Which levels of organization are present? A. Primary and quaternary, but no tertiary B. Primary, secondary and tertiary C. Secondary and…
- Materiał graficzny
Zadanie 7
(a) Describe protein structure, distinguishing shared features from features that can vary. (b) Explain how proteins enable substances to move across cell membranes.
Zadanie 24
A functional archaeal membrane pump is formed from one folded polypeptide chain. What is the highest level of protein structure present in that single-chain protein? A. Primary only B. Secondary only C. Tertiary D. Quaternary
Zadanie 28
Which levels of protein structure are visible in this representation? A. Secondary and tertiary B. Quaternary only C. Primary sequence only, with no folding D. Quaternary and a lipid bilayer
- Materiał graficzny