Explain membrane structure and evaluate passage evidence
Repair membrane regions and distinguish routes from measured transport.
Learning outcome: Connect membrane structure with selective permeability and identify controls for causal claims.
Starting recap
A route, a driving force and a measured rate are different information.
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Try
Small Na⁺ is strongly restricted by the lipid interior; uncharged glucose remains polar.
Open the experimentPredict
Predict channel surface properties and whether aquaporin establishes an O₂ effect.
Experiment
Compare four molecules in protein-free and specified-route contexts. Capture a contrast, repair a diagram and propose a matched control for one fictional comparison.
Inspect membrane features and passage evidence
Reference constraints · fictional evidence cases · Reference constraints and explicitly fictional qualitative comparisons, not a permeability simulation or measured dataset. Size, polarity, charge, membrane composition, protein identity/state, gradients, temperature, area and integrity matter. No numerical flux, direction, membrane voltage, ATP cost or elapsed time is inferred. Protein presence does not establish active transport; strongly restricted passage is not mathematically zero.
Reset keeps your prediction, captures and practice history.
Which feature supports the passage claim?
Choose a molecule and evidence context, predict a supported conclusion, then inspect the explanation. These controls select supplied cases; they do not run transport or change the fixed cell-reference diagram.
Water: Specified protein route. Evidence type: reference constraints; no measurement. Molecular class: small; polar or charged; net charge 0 in elementary-charge units.
- A functional aquaporin water pathway is stipulated.
- No quantitative transport assay or driving conditions are supplied.
Check what this evidence supports
An aquaporin supplies an additional water route. Its presence alone supplies neither a numerical rate nor the direction of net water movement.
Not established: The supplied structure establishes an exact rate, net direction or energy requirement.
A discriminating next comparison: Specify matched membrane composition/area, temperature, gradients, integrity and observation interval; compare the relevant route intervention with a control.
Numerical flux, net direction and energy cost are unavailable, not zero. A possible route is different from a measured passage rate; permeability alone does not establish net movement.
Fixed reference: an animal-cell plasma membrane
This original fluid-mosaic schematic is a structural reference for every selected case. It is not the protein-free experimental membrane. Sizes, spacing and numbers are illustrative; no motion or molecular trajectory is computed.
- Amphipathic phospholipids place aqueous-facing heads outside the tail-rich core. The two leaflets can differ in composition.
- Transmembrane proteins expose nonpolar regions toward lipid tails and polar regions toward water. A pore's polar lining faces water inside a protein; “inside the membrane” does not mean every local environment is hydrophobic.
- Peripheral proteins associate with a surface or another protein without necessarily spanning the bilayer. Anchoring can constrain movement.
- Cholesterol's OH region lies near polar heads, while its hydrophobic framework lies among tails. Effects on organization depend on temperature and composition; “always increases fluidity” is unsupported.
- Glycoprotein and glycolipid carbohydrate chains are shown extracellularly in this plasma-membrane reference. They can support recognition and interactions; they are not generic cytosolic decorations.
- Lateral mobility is movement within the membrane plane, not automatic flipping between leaflets. Components may be confined or attached; a fluid membrane is not unrestricted motion of every component.
Repair a diagram: a charged lipid-facing patch and a cytosolic glycan
Place the specified carbohydrate chain on the extracellular side of this reference. For the protein, identify which region contacts lipid tails and which contacts water: the usual exposed nonpolar surface belongs against the tail-rich core, while a polar pore lining faces its aqueous passage. This is a topology explanation, not a claim that every charged residue is absent from all membrane proteins.
Separate experimental reference: protein-free bilayer
| Molecule | Net charge (elementary-charge units) | Direct lipid route | Interpretation |
|---|---|---|---|
| O₂ | 0 | favored | Small nonpolar O₂ can partition into the lipid core and cross by direct diffusion. This supplies no numerical rate or net direction. |
| Water (selected) | 0 | possible | Water is small and polar. Some direct bilayer passage is possible; polar does not mean absolutely excluded. |
| Na⁺ | 1 | strongly-restricted | Charge and its aqueous interactions make direct passage through the hydrophobic core strongly unfavorable despite the ion being small. |
| Glucose | 0 | strongly-restricted | Glucose is uncharged but has multiple polar groups. Direct lipid passage is strongly restricted; net charge zero does not imply nonpolar. |
Size and charge are separate variables: small Na⁺ is strongly restricted, small polar water can cross to some extent, and uncharged glucose remains polar. A protein route must match the molecule. Protein-free does not mean impermeable to everything, and strongly restricted is not an exact zero.
Separate plant-envelope inset: wall and membrane
The wall helps protect and support the cell and resist expansion as water enters; its structure can also restrict passage. It is not an unrestricted sieve or a replacement for the plasma membrane. Animal cells do not have this cell wall. This inset calculates neither turgor nor water potential.
Evidence for a model, not motion inferred from a cartoon
Frye and Edidin studied intermixing of cell-surface antigens after mouse–human cell fusion. That supports lateral redistribution of the examined surface markers; it does not establish unrestricted motion of every membrane component. No experimental time series is reproduced here. Preston and colleagues tested a water-channel hypothesis by expressing CHIP28 in Xenopus oocytes; the reference supports investigating a protein route, not the fictional case's unmeasured numerical effect.
- Singer and Nicolson (1972): original fluid-mosaic model
- Frye and Edidin (1970): surface-antigen intermixing
- Preston and colleagues (1992): CHIP28 water-channel experiment
- Membrane-transport reference explanation
Reference constraints and explicitly fictional qualitative comparisons, not a permeability simulation or measured dataset. Size, polarity, charge, membrane composition, protein identity/state, gradients, temperature, area and integrity matter. No numerical flux, direction, membrane voltage, ATP cost or elapsed time is inferred. Protein presence does not establish active transport; strongly restricted passage is not mathematically zero.
Water — Specified protein route.
An aquaporin supplies an additional water route. Its presence alone supplies neither a numerical rate nor the direction of net water movement. Reference constraints and explicitly fictional qualitative comparisons, not a permeability simulation or measured dataset. Size, polarity, charge, membrane composition, protein identity/state, gradients, temperature, area and integrity matter. No numerical flux, direction, membrane voltage, ATP cost or elapsed time is inferred. Protein presence does not establish active transport; strongly restricted passage is not mathematically zero.
Captures retain the selected molecule and supplied evidence case. Replay restores reference constraints and fictional premises; it creates no measured permeability, transport event or independent replicate.
Understand
Apply
Public practice checks a specific claim. It does not establish independent mastery.
Separate a structural explanation from a measured effect. Explain why a wall cannot replace the membrane.
Continue
Completion requires a saved prediction, at least one capture and a reflection. Presence checks do not grade your reasoning.
Skipping retains experiments and awards no mastery.
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