B1 Form and function: Molecules Flashcards

1
Q

How are macromolecules produced from monomers?

A

Through condensation reactions, which link monomers together by removing a water molecule each time a bond forms.

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2
Q

How are polymers broken down into monomers?

A

Through hydrolysis reactions, which add water to break the bonds between monomers.

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3
Q

What are the form and function of monosaccharides?

A

Monosaccharides are single sugar units (like glucose, fructose).
They’re quick energy sources, soluble in water, and used in respiration and building larger carbohydrates.

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4
Q

What are polysaccharides used for?

A

Polysaccharides like starch, glycogen, and cellulose are used for energy storage and structural support.
Long chains = slow digestion = energy reserves.

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5
Q

How does cellulose’s structure relate to its role in plants?

A

Cellulose is made of beta-glucose, forming straight, unbranched chains linked by hydrogen bonds → strong microfibrils → rigid cell walls.

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6
Q

What role do glycoproteins play in cells?

A

They’re proteins with attached carbohydrates, found on cell surfaces, used for cell–cell recognition, signaling, and immune response.

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7
Q

How are triglycerides and phospholipids formed?

A

Both are made by condensation reactions:

Triglycerides = glycerol + 3 fatty acids

Phospholipids = glycerol + 2 fatty acids + 1 phosphate group

Water is removed at each link.

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8
Q

What’s the difference between saturated, monounsaturated, and polyunsaturated fatty acids?

A

Saturated: no double bonds

Monounsaturated: 1 double bond

Polyunsaturated: 2+ double bonds

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9
Q

What do triglycerides do in adipose tissue?

A

They store long-term energy and provide thermal insulation.

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10
Q

How do phospholipids form bilayers?

A

They self-arrange into bilayers in water:

Hydrophilic heads face water

Hydrophobic tails hide inside

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11
Q

Why can steroids pass through membranes easily?

A

They are non-polar lipids, so they can slip through the hydrophobic interior of the phospholipid bilayer.

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12
Q

What’s the general structure of an amino acid?

A

Central carbon

Amino group (–NH₂)

Carboxyl group (–COOH)

Hydrogen atom

R-group (variable side chain)

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13
Q

How are dipeptides and proteins formed?

A

By condensation reactions between amino acids, forming peptide bonds.
2 amino acids = dipeptide
Many = polypeptide or protein

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14
Q

Why do we need amino acids in our diet?

A

Some amino acids are essential—the body can’t make them, so we must get them from food.
(Essential ≠ important; it means you can’t build them yourself.)

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15
Q

How do pH and temperature affect protein structure?

A

They can disrupt hydrogen and ionic bonds, leading to denaturation—loss of shape and function.
High temps = unfold
Wrong pH = bond breakage

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16
Q

What causes the diversity in protein shapes?

A

The R-groups of amino acids have different properties (polar, non-polar, charged, etc.), which influence folding and function.
R-group variety = form diversity = function diversity

17
Q

How does the primary structure affect a protein?

A

The order of amino acids (primary structure) determines how the protein folds, and thus its final shape and function.
A single swap can ruin everything (e.g. sickle cell disease)

18
Q

What are the forms of secondary structure in proteins?

A

Alpha helices (coils)

Beta-pleated sheets (zig-zags)

Formed by hydrogen bonding

19
Q

What stabilizes a protein’s tertiary structure?

A

Hydrogen bonds

Ionic bonds

Disulfide bridges

Hydrophobic interactions

20
Q

How do polar and non-polar amino acids affect tertiary structure?

A

Non-polar R-groups hide inside (away from water)

Polar R-groups face outside

This folding pattern stabilizes the protein’s shape in water-based environments.

21
Q

What’s the difference between quaternary structure in conjugated and non-conjugated proteins?

A

Non-conjugated: 2+ polypeptide chains

Conjugated: includes prosthetic groups (e.g. heme in hemoglobin)