Assignment 1: Biology Article

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ch_2_-_molecules_of_life.pptx

drain cleaner

bleach

oven cleaner

hair remover

more basic

household ammonia

milk of magnesia hand soap

toothpaste

Tums detergents baking soda

seawater

egg white blood, tears

pure water

milk butter corn

urine, tea, typical rain black coffee

bread

beer

bananas

tomatoes, wine

orange juice

more acidic

vinegar

cola lemon juice

acid rain

gastric fluid

battery acid

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3

2

1

0

Figure 2.12 A pH scale. Here, red dots signify

hydrogen ions (H+) and blue dots signify hydroxyl

ions (OH–). Also shown are the approximate pH

values for some common solutions.

This pH scale ranges from 0 (most acidic) to 14

(most basic). A change of one unit on the scale

corresponds to a tenfold change in the amount

of H+ ions.

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Inorganic Molecules

Water

Oxygen

Carbon Dioxide

Salts

Organic Molecules

Carbohydrates

Lipids

Proteins

Nucleic Acids

C

C

C

C

C

C

C

C

C

C

C

C

H

H

H

H

H

H

H

H

H

H

H

H

H

H

H

H

H

H

H

H

C

H

C

H

C

H

H

C

H

H

H

H

H

H

C

C

H

H

C

H

H

C

H

H

Organic Molecules

Condensation

Figure 2.15 Animated!

Metabolism: two common reactions by

which cells build and break down organic

molecules.

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Hydrolysis

Figure 2.15 Animated!

Metabolism: two common reactions by

which cells build and break down organic

molecules.

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Carbohydrates

Monomer = simple sugar (monosaccharide)

Polymers = disaccharides or polysaccharides

Cellulose

Starch

Glycogen

Figure 2.16 Animated! Three of the

most common complex carbohydrates and their

locations in a few organisms. Each polysaccharide

consists only of glucose units, but different

bonding patterns that link the subunits result in

substances with very different properties.

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Lipids

Insoluble in water = Hydrophobic

hydrophobic “tail”

A) stearic acid (saturated)

B) linoleic acid (omega-6)

C) linolenic acid (omega-3)

D) oleic acid (cis)

E) elaidic acid (trans)

“head” (hydrophilic carboxyl group)

Figure 2.17 Animated! Fatty acids. Double bonds in the tails are colored red.

A The tail of stearic acid is fully saturated with hydrogen atoms. B Linoleic acid, with two double

bonds, is unsaturated. The first double bond occurs at the sixth carbon from the end of the tail, so

linoleic acid is called an omega-6 fatty acid. Omega-6 and C omega-3 fatty acids are “essential fatty

acids,” which means your body does not make them and they must come from food.

D The hydrogen atoms (in blue) around the double bond in oleic acid are on the same side of the tail.

Most other naturally occurring unsaturated fatty acids have these cis bonds. E Hydrogenation creates

abundant trans bonds, with hydrogen atoms on opposite sides of the tail (in blue).

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hydrophilic head

two hydrophobic tails

A phospholipid molecule

Figure 2.18 Phospholipids as components of cell membranes. A double layer of

phospholipids—the lipid bilayer—is the structural foundation of all cell membranes.

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Figure 2.18 Phospholipids as components of cell membranes. A double layer of

phospholipids—the lipid bilayer—is the structural foundation of all cell membranes.

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an estrogen

testosterone

female

wood duck

male

wood duck

Figure 2.19 Estrogen and testosterone, steroid

hormones that cause different traits to arise in males

and females of many species such as wood ducks.

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Proteins

Monomer = amino acids

Polymers = proteins

Figure 2.20 Animated! How protein structure arises. Chapter 7 returns to protein synthesis.

1 A peptide bond forms between two

amino acids (here, methionine and valine).

2 More amino acids become linked into a

polypeptide chain. The sequence of amino

acids in the chain is the protein’s primary

structure. Each type of protein has a unique

primary structure.

3 Secondary structure

arises as the polypeptide

twists into a coil or sheet

held in place by hydrogen

bonds. Most proteins

have coils and sheets.

4 Tertiary structure occurs

when the coils and sheets

fold up into a domain. In

this example, the coils of a

globin chain form a pocket.

5 Some proteins have two or more

polypeptide chains. Hemoglobin,

shown here, consists of four globin

chains ( green and blue). Each globin

pocket now holds a heme group (red ).

6 Fibrous proteins aggregate by the

many thousands into much larger

structures. The filaments that make

up hair are examples; they consist of

tightly bundled keratin proteins.

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Figure 2.20 Animated! How protein structure arises. Chapter 7 returns to protein synthesis.

1 A peptide bond forms between two

amino acids (here, methionine and valine).

2 More amino acids become linked into a

polypeptide chain. The sequence of amino

acids in the chain is the protein’s primary

structure. Each type of protein has a unique

primary structure.

3 Secondary structure

arises as the polypeptide

twists into a coil or sheet

held in place by hydrogen

bonds. Most proteins

have coils and sheets.

4 Tertiary structure occurs

when the coils and sheets

fold up into a domain. In

this example, the coils of a

globin chain form a pocket.

5 Some proteins have two or more

polypeptide chains. Hemoglobin,

shown here, consists of four globin

chains ( green and blue). Each globin

pocket now holds a heme group (red ).

6 Fibrous proteins aggregate by the

many thousands into much larger

structures. The filaments that make

up hair are examples; they consist of

tightly bundled keratin proteins.

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Figure 2.20 Animated! How protein structure arises. Chapter 7 returns to protein synthesis.

1 A peptide bond forms between two

amino acids (here, methionine and valine).

2 More amino acids become linked into a

polypeptide chain. The sequence of amino

acids in the chain is the protein’s primary

structure. Each type of protein has a unique

primary structure.

3 Secondary structure

arises as the polypeptide

twists into a coil or sheet

held in place by hydrogen

bonds. Most proteins

have coils and sheets.

4 Tertiary structure occurs

when the coils and sheets

fold up into a domain. In

this example, the coils of a

globin chain form a pocket.

5 Some proteins have two or more

polypeptide chains. Hemoglobin,

shown here, consists of four globin

chains ( green and blue). Each globin

pocket now holds a heme group (red ).

6 Fibrous proteins aggregate by the

many thousands into much larger

structures. The filaments that make

up hair are examples; they consist of

tightly bundled keratin proteins.

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Nucleic Acids

Monomer = nucleotide

Polymers = DNA or RNA

ribose

sugar

base (adenine)

phosphate

groups

Figure 2.22 Nucleic acids.

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RNA

Figure 2.22 Nucleic acids.

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DNA

RNA

Figure 2.22 Nucleic acids.

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Figure 2.22 Nucleic acids.

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