quiz 3 study guide ] Flashcards

(92 cards)

1
Q

Why is water a liquid at room temperature?

A

Extensive hydrogen bonding between water molecules

Hydrogen bonds are responsible for many of water’s unique properties.

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2
Q

What bond holds atoms together within one water molecule?

A

Covalent O–H bonds (intramolecular)

These bonds are strong and determine the molecular structure of water.

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3
Q

What interaction holds water molecules together with each other?

A

Hydrogen bonds (intermolecular)

These weak interactions are crucial for the properties of water.

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4
Q

Key distinction: covalent vs hydrogen bonds in water?

A

Covalent O–H bonds hold atoms within a molecule; hydrogen bonds between molecules determine physical properties

This distinction is fundamental in understanding molecular interactions.

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5
Q

Why does water have a high boiling point for its size?

A

Hydrogen bonding raises boiling point (100°C at 18 g/mol)

The extensive hydrogen bonding network requires more energy to break.

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6
Q

What is a hydrogen bond?

A

A weak electrostatic attraction between a donor H and an acceptor atom (O, N, or F)

Hydrogen bonds are essential in biological systems.

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7
Q

Hydrogen bond donor requirement?

A

H covalently bonded to O, N, or F

This configuration allows the hydrogen to participate in hydrogen bonding.

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8
Q

Hydrogen bond acceptor requirement?

A

O, N, or F with lone pairs

These atoms can stabilize the hydrogen bond through their electron pairs.

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9
Q

Strength order: covalent vs H-bond vs van der Waals?

A

Covalent strongest (~100 kcal/mol) > H-bond (2–5) > van der Waals (~1)

Understanding this order is crucial for predicting molecular interactions.

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10
Q

What must a molecule have to H-bond with itself?

A

Both a donor (O–H/N–H/F–H) AND an acceptor (O/N/F with lone pairs)

This requirement is key for self-association in molecules like water.

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11
Q

Why are hydrogen bonds important in biology?

A

They stabilize biomolecule structure but allow flexibility

This balance is vital for the function of proteins and nucleic acids.

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12
Q

Main types of noncovalent interactions in biomolecules?

A
  • Hydrogen bonds
  • Electrostatic interactions
  • Van der Waals forces
  • Hydrophobic interactions

These interactions play critical roles in the structure and function of biomolecules.

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13
Q

Key difference: covalent vs noncovalent interactions?

A

Covalent = electron sharing; noncovalent = no electron sharing

This distinction is fundamental in chemistry.

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14
Q

Why are weak interactions useful for life?

A

Individually weak but collectively strong; allow dynamic and reversible structure/function

This property is essential for biological processes.

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15
Q

What is an acid?

A

Proton (H⁺) donor

Acids play a crucial role in chemical reactions and biological systems.

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16
Q

What is a base?

A

Proton (H⁺) acceptor

Bases are essential for neutralizing acids in biological systems.

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17
Q

What is the pH equation?

A

pH = −log[H⁺]

This equation is fundamental in understanding acidity and basicity.

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18
Q

What does low pH mean?

A

High [H⁺] (acidic)

Low pH values indicate strong acidic conditions.

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19
Q

What does high pH mean?

A

Low [H⁺] (basic)

High pH values indicate basic conditions.

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20
Q

How much does [H⁺] change per 1 pH unit?

A

10-fold

This logarithmic scale is crucial for understanding acidity.

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21
Q

Neutral pH at 25°C?

A

pH = 7

This is the standard reference point for acidity.

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22
Q

What is a buffer?

A

A system that resists pH change when acid/base is added

Buffers are critical for maintaining stable pH in biological systems.

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23
Q

What does a buffer contain?

A
  • Weak acid (HA)
  • Conjugate base (A⁻)

This combination allows buffers to neutralize added acids or bases.

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24
Q

What does HA do in a buffer?

A

Neutralizes added base

This action helps maintain pH stability.

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25
What does **A⁻** do in a buffer?
Neutralizes added acid ## Footnote This action is essential for pH regulation.
26
What determines **buffering capacity**?
Total concentration of buffer components ## Footnote Higher concentrations allow for greater resistance to pH changes.
27
When is buffering **maximal**?
When [HA] = [A⁻] (pH = pKa) ## Footnote This condition provides optimal buffering ability.
28
Typical effective **buffer range**?
pKa ± 1 pH unit ## Footnote Buffers are most effective within this range.
29
Main **blood buffer systems**?
* Bicarbonate (~75%) * Proteins (~25%) * Phosphate (more intracellular) ## Footnote These systems are crucial for maintaining blood pH.
30
Why is **bicarbonate buffer** most important in blood?
High [HCO₃⁻], open system (CO₂ exhaled), regulated by lungs (fast) + kidneys (slow) ## Footnote This system plays a vital role in acid-base balance.
31
Bicarbonate buffer **equilibrium**?
CO₂ + H₂O ⇌ H₂CO₃ ⇌ H⁺ + HCO₃⁻ ## Footnote This reaction illustrates the dynamic nature of the bicarbonate buffer system.
32
What is meant by **“open system”** for bicarbonate buffer?
CO₂ can be removed by exhaling ## Footnote This property allows for rapid adjustments in pH.
33
What does **hyperventilation** do to blood pH?
Increases pH (respiratory alkalosis) ## Footnote This condition results from excessive CO₂ removal.
34
Why does **hyperventilation** raise pH?
Blows off CO₂ → shifts equilibrium left → decreases [H⁺] ## Footnote This shift results in a higher pH.
35
What does **hypoventilation** do to blood pH?
Decreases pH (respiratory acidosis) ## Footnote This condition results from CO₂ retention.
36
Why does **hypoventilation** lower pH?
Retains CO₂ → shifts equilibrium right → increases [H⁺] ## Footnote This shift results in a lower pH.
37
Panic attack **hyperventilation** causes what?
Respiratory alkalosis (tingling/lightheadedness) ## Footnote This condition can lead to discomfort and anxiety.
38
Paper bag breathing helps because…
Increases CO₂ intake ## Footnote This method can alleviate symptoms of hyperventilation.
39
What are **colligative properties**?
Properties that depend on number of dissolved particles, not identity ## Footnote These properties are important in solutions and biological systems.
40
What is **osmolarity**?
Total concentration of dissolved particles ## Footnote Osmolarity is a key factor in understanding solution behavior.
41
Osmolarity **formula**?
Osmolarity = molarity × number of particles after dissociation ## Footnote This formula is essential for calculating osmotic pressure.
42
Example: 0.25 M **Na₃PO₄** osmolarity?
0.25 × 4 = 1.0 osmolar ## Footnote This calculation illustrates the concept of osmolarity.
43
Molarity vs **osmolarity**?
Molarity = concentration of molecules; osmolarity = concentration of total particles ## Footnote Understanding this difference is crucial for solution chemistry.
44
Osmolarity vs **tonicity**?
Osmolarity counts particles; tonicity predicts cell effect (depends on membrane permeability) ## Footnote This distinction is important in biological contexts.
45
Normal **blood osmolarity**?
~0.3 osmolar (300 mOsm) ## Footnote This value is critical for physiological function.
46
Hypertonic solution does what to **cells**?
Cells shrink (crenation) ## Footnote This occurs due to water moving out of the cells.
47
Hypotonic solution does what to **cells**?
Cells swell (lysis) ## Footnote This occurs due to water moving into the cells.
48
Why must **IV solutions** be isotonic?
Prevent cell damage from water movement ## Footnote Isotonic solutions maintain cellular integrity.
49
What does **amphipathic** mean?
Has both hydrophobic and hydrophilic regions ## Footnote This property is crucial for membrane formation.
50
Amphipathic molecule **hydrophobic region**?
Long hydrocarbon tail (typically 8–18 carbons) ## Footnote This region is nonpolar and repels water.
51
Amphipathic molecule **hydrophilic region**?
Polar/charged head group ## Footnote This region interacts favorably with water.
52
What is a **micelle**?
Amphipathic molecules forming a sphere with tails inside and heads outside ## Footnote Micelles are important in solubilizing fats.
53
What triggers **micelle formation**?
Concentration above the CMC (critical micelle concentration) ## Footnote This concentration is necessary for micelle stability.
54
Why do **micelles** form in water?
Hydrophobic effect ## Footnote This effect drives the aggregation of nonpolar regions.
55
Examples of **amphipathic molecules**?
* Fatty acids/soaps * Detergents (SDS) * Bile salts ## Footnote These molecules play critical roles in biological processes.
56
Biological importance of **amphipathic molecules**?
* Membrane formation * Detergent solubilization * Bile salt fat emulsification ## Footnote These functions are essential for digestion and cellular structure.
57
What is the **hydrophobic effect**?
Nonpolar molecules aggregate in water because water entropy increases ## Footnote This effect is fundamental in biological systems.
58
Is the **hydrophobic effect** due to attraction between nonpolar molecules?
No—it's driven by increased entropy of released water ## Footnote This understanding is crucial for molecular interactions.
59
Why do **nonpolar molecules** “cluster” in water?
Aggregation releases ordered water “cages,” increasing entropy ## Footnote This clustering is a key aspect of the hydrophobic effect.
60
What happens to **ΔG** when hydrophobic groups aggregate?
ΔG becomes negative (favorable) ## Footnote This indicates that the process is thermodynamically favorable.
61
Hydrophobic effect is mainly **entropy-driven** or **enthalpy-driven**?
Entropy-driven ## Footnote This characteristic is essential for understanding molecular behavior.
62
Biological roles of **hydrophobic effect**?
* Protein folding * Membrane bilayers * Protein binding * Enzyme-substrate binding * Drug-receptor binding ## Footnote These roles are critical for biological function.
63
Water **autoionization reaction** (simple form)?
H₂O ⇌ H⁺ + OH⁻ ## Footnote This reaction is fundamental to acid-base chemistry.
64
More accurate **autoionization reaction**?
2 H₂O ⇌ H₃O⁺ + OH⁻ ## Footnote This representation emphasizes the role of hydronium ions.
65
What is **Kw**?
Kw = [H⁺][OH⁻] ## Footnote This product is constant at a given temperature.
66
Kw value at **25°C**?
1.0 × 10⁻¹⁴ ## Footnote This value is crucial for calculating pH and pOH.
67
[H⁺] and [OH⁻] in **pure water at 25°C**?
Both 1.0 × 10⁻⁷ M ## Footnote This equality defines neutral conditions.
68
What is **pOH**?
pOH = −log[OH⁻] ## Footnote This measure is related to pH and acidity.
69
Relationship between **pH and pOH** at 25°C?
pH + pOH = 14 ## Footnote This relationship is fundamental in acid-base chemistry.
70
In any aqueous solution, what stays constant at **25°C**?
[H⁺][OH⁻] = 1.0 × 10⁻¹⁴ ## Footnote This constant is essential for understanding solution behavior.
71
Neutral means what?
[H⁺] = [OH⁻] ## Footnote This condition defines neutrality in solutions.
72
Why isn’t **neutral** always pH 7?
Kw changes with temperature ## Footnote This variation affects the definition of neutrality.
73
Neutral pH at **37°C** (body temp) is about…
~6.8 (because Kw is higher) ## Footnote This adjustment is important for physiological processes.
74
What is **Ka**?
Acid dissociation constant: Ka = [H⁺][A⁻]/[HA] ## Footnote This constant quantifies the strength of an acid.
75
What is **pKa**?
pKa = −log(Ka) ## Footnote This measure is used to express acid strength.
76
Low **pKa** means…
Stronger acid (donates H⁺ easily) ## Footnote This relationship is crucial for understanding acid behavior.
77
High **pKa** means…
Weaker acid (reluctant to donate H⁺) ## Footnote This indicates a lower tendency to ionize.
78
Henderson–Hasselbalch **equation**?
pH = pKa + log([A⁻]/[HA]) ## Footnote This equation is essential for buffer calculations.
79
When pH = pKa, what is the ratio **[A⁻]/[HA]**?
1 (equal concentrations) ## Footnote This condition indicates optimal buffering.
80
When pH > pKa, which form predominates?
A⁻ (deprotonated, conjugate base) ## Footnote This shift is important for understanding acid-base behavior.
81
When pH < pKa, which form predominates?
HA (protonated, conjugate acid) ## Footnote This condition indicates a higher concentration of the acid form.
82
Buffer **selection rule**?
Choose buffer with pKa within ±1 of desired pH ## Footnote This guideline ensures effective buffering.
83
Rule of thumb: 2 pH units below **pKa** means…
~99% HA (protonated) ## Footnote This rule helps predict acid-base behavior.
84
Rule of thumb: 2 pH units above **pKa** means…
~99% A⁻ (deprotonated) ## Footnote This rule is useful for understanding buffer systems.
85
Histidine side chain **pKa** is about…
~6.0 (imidazole) ## Footnote This property is important for enzyme function.
86
Why is **histidine** important in enzymes?
Can donate/accept protons near physiological pH ## Footnote This flexibility is crucial for catalytic activity.
87
Phosphate buffer **pKa** (given) and where important?
pKa = 6.8; important intracellularly ## Footnote This buffer system plays a key role in cellular processes.
88
Bicarbonate buffer **pKa** and blood ratio at pH 7.4?
pKa = 6.1; [HCO₃⁻]/[H₂CO₃] ≈ 20:1 ## Footnote This ratio is vital for maintaining blood pH.
89
Common mistake: **pKa vs pH**?
pKa is property of an acid; pH is property of a solution ## Footnote This distinction is essential for understanding acid-base chemistry.
90
Can you use **Henderson–Hasselbalch** for strong acids?
No—only valid for weak acids/buffers ## Footnote Strong acids do not establish a stable equilibrium.
91
Why can log([A⁻]/[HA]) be **negative**?
When [A⁻] < [HA] (pH < pKa) ## Footnote This situation indicates a predominance of the protonated form.
92
Do all **buffers** work at all pH values?
No—must be within pKa ± 1 ## Footnote This limitation is crucial for effective buffering.