Protein Binding, Osmosis, and Body Fluids (Physiology)

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A comprehensive set of practice flashcards covering protein binding (specificity, affinity, Keq, Kd, inhibitors, agonists/antagonists), IV fluid pharmacology (osmolarity, tonicity, penetrating vs nonpenetrating solutes, calculation steps), body fluid compartments (ICF/ECF, plasma, interstitial fluid), osmosis and osmolarity concepts, and foundational tissue and membrane physiology (epithelial/connective tissues, CAMs, ECM, resting membrane potential, Nernst and GHK equations).

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41 Terms

1
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What is specificity in protein–ligand binding?

The ability of a protein to bind to a particular ligand or to a group of closely related ligands.

2
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What is required for ligand binding besides specificity?

Molecular complementarity, often with an induced-fit interaction between protein and ligand.

3
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What does affinity refer to in protein–ligand interactions?

The degree to which a protein remains attached to a ligand.

4
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What does equilibrium mean in protein-binding reactions?

The rate of binding equals the rate of unbinding (dynamic balance).

5
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What does a high Keq indicate about ligand binding?

A strong tendency for the ligand and protein to form the bound complex (high affinity).

6
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What does a large Kd indicate about ligand binding?

Weak affinity; a larger proportion of ligand and protein remain unbound at equilibrium.

7
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How are Keq and Kd related?

They are inversely related; a high Keq corresponds to a low Kd.

8
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Which implies stronger binding, high Keq or low Kd?

High Keq and low Kd both indicate strong binding between protein and ligand.

9
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How do competitive and allosteric inhibitors differ in where they bind?

Competitive inhibitors bind at the active site; allosteric inhibitors bind at a different (allosteric) site.

10
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What is the difference between an agonist and an antagonist?

An agonist increases receptor activity; an antagonist decreases activity or blocks it.

11
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What is an inhibitor in enzyme–ligand chemistry?

A molecule that reduces the rate of enzyme activity or receptor activation, either by competitive or allosteric mechanisms.

12
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Where does a competitive inhibitor bind?

At the enzyme’s active site (the same site as the substrate).

13
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Where does an allosteric inhibitor bind?

At an allosteric site away from the active site, changing enzyme/receptor activity.

14
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What does 'saturation' mean in receptor–ligand binding?

All receptors are occupied; adding more ligand does not increase the response.

15
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What are the two major fluid compartments in the body?

Intracellular fluid (ICF) and extracellular fluid (ECF).

16
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How is extracellular fluid subdivided?

Into plasma (intravascular) and interstitial fluid.

17
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What drives water movement during osmosis?

A solute concentration gradient across a semipermeable membrane.

18
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What is osmotic pressure?

The pressure required to oppose osmosis.

19
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What is osmolarity?

The number of osmotically active particles per liter of solution.

20
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What is osmolality?

Osmolarity expressed per kilogram of solvent; practically interchangeable in physiology.

21
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Which solutes are penetrating versus nonpenetrating?

Penetrating solutes (e.g., glucose, urea) cross membranes; nonpenetrating solutes (e.g., NaCl) largely do not.

22
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In IV calculations, what is the recommended first step?

Work the total body column by adding nonpenetrating solutes and volume; ignore penetrating solutes until later steps.

23
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How are IV solutions categorized in Table 5.5?

By osmolarity and tonicity (isosmotic, hyperosmotic, isotonic, hypotonic, etc.).

24
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What is tonicity?

The effect of a solution on cell volume due to nonpenetrating solutes; hypertonic draws water out, hypotonic causes swelling.

25
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How do penetrating solutes affect tonicity versus osmolarity?

Penetrating solutes can alter osmolarity but may not change tonicity if they distribute evenly between ECF and ICF.

26
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What is the basal lamina?

The basement membrane secreted by epithelial cells that anchors epithelia to underlying tissue.

27
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What is lumen?

The inside space of a tubular structure; some lumens are considered outside the body.

28
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What are the five epithelial tissue types?

Secretory, Protective, Exchange, Ciliated, and Transport epithelia.

29
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What are the four basic tissue types?

Epithelial, Connective, Muscle, and Nerve tissues.

30
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What are CAMs and give examples?

Cell adhesion molecules; examples include Cadherins, Integrins, Immunoglobulin superfamily CAMs, and Selectins.

31
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What are the three components of connective tissue?

Ground substance (ECM), cells (e.g., fibroblasts, blasts, cytes), and matrix fibers (collagen, elastin, fibrillin, fibronectin).

32
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What does the extracellular matrix (ECM) consist of broadly?

Proteoglycans and insoluble protein fibers (e.g., collagen, fibronectin, laminin) surrounding cells.

33
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Which tissues are excitable?

Muscle tissue (excitable for contraction) and neural tissue (neurons are excitable).

34
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What creates the resting membrane potential?

Ion gradients and selective membrane permeability, largely due to K+ leak channels and Na+/K+ ATPase activity.

35
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What are the typical equilibrium potentials for K+ and Na+?

K+ ~ -90 mV; Na+ ~ +35 mV, illustrating their opposing gradients.

36
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What equation is used to calculate the equilibrium potential for a single ion?

The Nernst equation.

37
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What equation estimates membrane potential when multiple ions contribute?

The Goldman–Hodgkin–Katz (GHK) equation.

38
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What happens when K+ channels open in a resting cell?

K+ ions leave the cell, making the inside more negative (hyperpolarization).

39
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What is the electrochemical gradient?

The combined influence of concentration (chemical) gradient and electrical gradient on ion movement.

40
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What is the purpose of the Goldman–Hodgkin–Katz equation?

To estimate the actual resting membrane potential when multiple ions contribute.

41
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How do ions move when the membrane is permeable to K+ and Na+ differently?

Movement is governed by both concentration and electrical gradients, creating the electrochemical gradient.