Honors Biology - The Working Cell Test

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Severn School Honors Bio

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21 Terms

1
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fluid mosaic model

  • used to describe structure of plasma membrane (phospholipid bilayer) as fluid + mosaic

  1. fluid

    1. fatty acid chains → plasma membrane contains a mix of both saturated and unsaturated fa. chains → allows for permiability (not too close to be solid; not too far for LDFs)

    2. cholesterol is a lipid = hydrophobic molecule → function is to stabilize the molecule (in cold, risk of getting solid so cholesterol physicallly blocks from getting too close) (in warm, risk of moving away→ no LDFs, so cholesterol holds together

  2. mosaic → made up of many small parts like phospholipids, cholesterol, and proteins

<ul><li><p>used to describe structure of plasma membrane (phospholipid bilayer) as fluid + mosaic</p></li></ul><ol><li><p><strong>fluid </strong></p><ol><li><p><u>fatty acid chains </u>→ plasma membrane contains a mix of both saturated and unsaturated fa. chains → allows for permiability (not too close to be solid; not too far for LDFs)</p></li><li><p><u>cholesterol </u><em>→ </em>is a lipid = hydrophobic molecule → function is to stabilize the molecule (in cold, risk of getting solid so cholesterol physicallly blocks from getting too close) (in warm, risk of moving away→ no LDFs, so cholesterol holds together</p></li></ol></li><li><p><strong>mosaic → </strong>made up of many small parts like phospholipids, cholesterol, and <u>proteins</u></p></li></ol><p></p>
2
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plasma membrane is _____

selectively permeable, meaning that only certain substances can cross: small nonpolar molecules

energy barrier

<p>selectively permeable, meaning that only certain substances can cross: small nonpolar molecules</p><p><em>energy barrier</em></p>
3
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transport proteins

  • allow specific ions or molecules to enter/exit the cell

  • uncharged solutes can easily pass w/ out help of a protein important (ex. O2→ required in cell respiration)

  • charged solutes require help from transport proteins (specific to each ion/molecule)

4
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enzymes

  • function: to speed up/catalyze chemical RXNS

  • some membrane proteins are enzymes

  • ex. mitochondria had enzymes on interior membrane (cristae); more membrane → more enz. → more ATP

5
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attachment proteins

  • attach to ECM and cytoskeleton

  • help to support the membrane

  • can coordinate external + internal changes

  • ex. intergin protein

6
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receptor proteins

  • receptors that allow a cell to receive a signal

  • used to detect glycoproteins on other cells

7
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junction proteins

  • form intercellular juntions that attach adjacent cells

  • ex. tight, anchoring, and gap

8
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glycoproteins

  • polypeptide modified in RER w/ sugar molecs

  • serves as ID tags, can be recognized by receptor proteins of other cells

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Passive Transport (diffusion)

  • spontaneous movement of a substance from an area with high concentration to one with low concentration (can occur w/out a membrane)

  • does not require energy

  • down the concentration gradient: [high] to [low]

  • simple diffusion → small, nonpolar molecules, channel proteins not used

  • facilitated diffusion → use channel proteins; for polar, small substances ex. channel proteins (specific molecules) and aquaporin

<ul><li><p>spontaneous movement of a substance from an area with high concentration to one with low concentration (can occur w/out a membrane)</p></li><li><p>does not require energy</p></li><li><p>down the concentration gradient: [high] to [low]</p></li><li><p><strong>simple diffusion </strong>→ small, nonpolar molecules, channel proteins not used</p></li><li><p><strong>facilitated diffusion → </strong>use channel proteins; for polar, small substances ex. channel proteins (specific molecules) and aquaporin</p></li></ul><p></p>
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Active Transport

  • transports small + charged particles

  • specific substances

  • used energy (ATP) → comes from ATP hydrolysis where energy stored in bonds is released (ATP→ADP+P)

  • protein pumps (transport protein)

  • against the concentration gradient: [low] → [high]

  • like an airlock

<ul><li><p>transports small + charged particles</p></li><li><p>specific substances</p></li><li><p>used energy (ATP) → comes from ATP hydrolysis where energy stored in bonds is released (ATP→ADP+P)</p></li><li><p>protein pumps (transport protein)</p></li><li><p>against the concentration gradient: [low] → [high]</p></li><li><p>like an airlock</p></li></ul><p></p>
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osmosis

  • diffusion of water from high water concentration to low water concentration across a selectively permeable membrane

  • see diagram on notes sheet 2

<ul><li><p>diffusion of water from high water concentration to low water concentration across a selectively permeable membrane</p></li><li><p>see diagram on notes sheet 2</p></li></ul><p></p>
12
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tonicity (hypotonic, isotonic, and hypertonic)

  • the ability of a surronding solution to cause a cell to gain or lose water

  • described by terms hypotonic, isotonic, and hypertonic

  • hypotonic solution → has a lower solute concetraction compared to that of another solution (water goes into cell); causes cell lysis in animal cells and turgid (normal) in plant cells

  • isotonic solution → has the same solute concentration as that of another solution (water goes in and out); normal for animal cells and flaccid for plant cells

  • hypertonic solution → has a higher solute concentration compared to that of another solution (water goes out of cell); causes shriveling in animal cells and plasmolysis (shriveled) in plant cells → pulls away from cell wall

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osmoregulation

  • some cells have mechanisms to survive hypo and hypertonic solutions

  • ex. contractile vacuoles → helps to maintain balance

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Exocytosis

  • function → to remove large/bulky materials (ex. large molecs, liquid, large material) from cell

  • transports nonspecifically

  • no gradient involved

  • Process → vesicles fuse with plasma membrane to release contents

  • energy required(to remodel cytoskeleton → NO QUESTIONS ABT)

<ul><li><p><strong>function → </strong>to remove large/bulky materials (ex. large molecs, liquid, large material) from cell</p></li><li><p>transports nonspecifically</p></li><li><p>no gradient involved</p></li><li><p><strong>Process </strong>→ vesicles fuse with plasma membrane to release contents</p></li><li><p>energy required(to remodel cytoskeleton → <strong>NO QUESTIONS ABT</strong>)</p></li></ul><p></p>
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Endocytosis

  • function →the process of taking in large/bulky materials (ex. large molecules, liquids) into the cell

  • phagocytosis → general term that means to bring large materials into the cell (energy req***)

    • transports non-specifically

    • no concentration gradient

    • does not use transport proteins → plasma membrane folds in on itself

  • receptor mediated endocytosis → brings large materials in attached to receptor proteins (energy req***)

    • transports specific substances (b/c uses receptor proteins)

    • no gradient

    • uses receptor proteins to bing to specific molecule then is engulfed

  • pinocytosis → purpose to bring liquids into the cell

    • no gradient

    • transports non-specifically

    • does not use transport proteins → plasma membrane folds in on itself

<ul><li><p><strong>function</strong> →the process of taking in large/bulky materials (ex. large molecules, liquids) into the cell</p></li><li><p><strong>phagocytosis →</strong> general term that means to bring large materials into the cell (energy req***) </p><ul><li><p><em>transports non-specifically</em></p></li><li><p>no concentration gradient</p></li><li><p>does not use transport proteins → plasma membrane folds in on itself</p></li></ul></li><li><p><strong>receptor mediated endocytosis → </strong>brings large materials in attached to receptor proteins (energy req***)</p><ul><li><p><em>transports <u>specific </u>substances</em> (b/c uses receptor proteins)</p></li><li><p>no gradient</p></li><li><p>uses receptor proteins to bing to specific molecule then is engulfed</p></li></ul></li><li><p><strong>pinocytosis</strong> → purpose to bring liquids into the cell</p><ul><li><p>no gradient</p></li><li><p><em>transports non-specifically</em></p></li><li><p>does not use transport proteins → plasma membrane folds in on itself</p></li></ul></li></ul><p></p>
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protein structure diagram types

  • ball and stick → shows outside characteristics, feeling for atom amounts and idividual atoms/bonds

  • space filling → shows arons and any empty space; area occupied by atoms

  • cartoon/ribbbon → show structural details and secondary structure

  • molecular surface → shows overall shape/topography and water accesibilty; surface R-groups

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Enzyme + Substrate Structure

  • fit structurally like a lock and key

  • active site → contains substrate binding site and catalytic site (where RXN occurs)

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induced fit

  • shape of the active site changes upon binding of the substrate

  • substrate induces a shape change b/c change in attractive forces (IMFs)

  • make it easier for RXNs to occur b/c substrate is more unstable

19
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activation energy

  • minimum amt of energy required for reactant molecules before they can undergo a chemical reaction

  • enzyme lowers this barrier to increase reaction rates, making processes more efficient.

  • see graph on page 3 notes 4

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How do enzymes catalyze reactions?

Enzymes catalyze reactions by lowering the activation energy needed for reactants to undergo a chemical reaction, allowing for faster reaction rates and increased efficiency. see page 4 notes 4

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Enzyme Inhibition

  • chemicals that interfere/inhibit enzyme activity; function reduced or completely gone

  • competitive inhibition → inhibitor blocks binding of substrate; substrate competes for active site; can be reversed by having excess substrate → out competes it

  • noncompetitive inhibition → inhibitor binds to the enzyme at the allosteric site which causes the active site to change shape, preventing substrate binding

  • can be intentional to control cellular metabolism (chem RXNS in cell) → see notes 5 diagram KNOW → negative feedback loop

  • can also be accidental ex. cyanide + hemaglobin

<ul><li><p>chemicals that interfere/inhibit enzyme activity; function reduced or completely gone</p></li><li><p><strong>competitive inhibition</strong> → inhibitor blocks binding of substrate; substrate <u>competes </u>for active site; <em>can be reversed by having excess substrate → out competes it</em></p></li><li><p><strong>noncompetitive inhibition </strong>→ inhibitor binds to the enzyme at the allosteric site which causes the active site to change shape, preventing substrate binding</p></li><li><p>can be intentional to control cellular metabolism (chem RXNS in cell) → see notes 5 diagram <strong>KNOW → </strong>negative feedback loop</p></li><li><p>can also be accidental ex. cyanide + hemaglobin</p></li></ul><p></p>