Fig. 3-00

Fig. 3-01

Carbon skeletons vary in length Carbon skeletons may have double bonds,which can vary in location

Carbon skeletons may be unbranched or branched Carbon skeletons may be arranged in rings

Double bond

Fig. 3-01a

Carbon skeletons vary in length

Fig. 3-01b

Double bondCarbon skeletons may have double bonds,

which can vary in location

Fig. 3-01c

Carbon skeletons may be unbranched or branched

Fig. 3-01d

Carbon skeletons may be arranged in rings

Fig. 3-02

Structural formula Ball-and-stick model Space-filling model

Fig. 3-02a

Structural formula

Fig. 3-02b

Ball-and-stick model

Fig. 3-02c

Space-filling model

Fig. 3-03

Fig. 3-04

Short polymer Monomer

Dehydrationreaction

Longer polymer

Hydrolysis

(a) Building a polymer chain (b) Breaking a polymer chain

Fig. 3-04a

Short polymer Monomer

Dehydrationreaction

Longer polymer

(a) Building a polymer chain

Fig. 3-04b

Hydrolysis

(b) Breaking a polymer chain

Fig. 3-05

Glucose Fructose

C6H12O6 C6H12O6

Isomers

Fig. 3-05a

Glucose Fructose

C6H12O6 C6H12O6

Isomers

Fig. 3-06

(a) Linear and ring structures

(b) Abbreviatedring structure

Fig. 3-06a

(a) Linear and ring structures

Fig. 3-06b

(b) Abbreviated ring structure

Fig. 3-07

Glucose Galactose

Lactose

Fig. 3-08

processed to extract

broken down into

converted to sweeter

added to foods ashigh-fructose corn syrup

Starch

Glucose

Fructose

Ingredients: carbonated water,high-fructose corn syrup,caramel color, phosphoric acid,natural flavors

Fig. 3-09

Glucosemonomer

(a) Starch

(b) Glycogen

(c) Cellulose

Starch granules

Glycogengranules

Cellulose fibril

Cellulosemolecules

Fig. 3-10

Oil (hydrophobic)

Vinegar (hydrophilic)

Fig. 3-11

Fatty acid

Glycerol

(a) A dehydration reaction linking a fatty acid to glycerol

(b) A fat molecule with a glycerol “head” and three energy-rich hydrocarbon fatty acid “tails”

Fig. 3-11a

Fatty acid

Glycerol

(a) A dehydration reaction linking a fatty acid to glycerol

Fig. 3-11b

(b) A fat molecule with a glycerol “head” and three energy-rich hydrocarbon fatty acid “tails”

Fig. 3-12

Saturated Fats

TYPES OF FATS

Unsaturated Fats

Margarine

Plant oils Trans fats Omega-3 fats

INGREDIENTS: SOYBEAN OIL, FULLY HYDROGENATED

COTTONSEED OIL, PARTIALLY HYDROGENATED

COTTONSEED OIL AND SOYBEAN OILS, MONO AND

DIGLYCERIDES, TBHO AND CITRIC ACID ANTIOXIDANTS

Fig. 3-12a

Saturated Fats

Fig. 3-12b

Unsaturated Fats

Margarine

Plant oils Trans fats Omega-3 fats

INGREDIENTS: SOYBEAN OIL, FULLY HYDROGENATED

COTTONSEED OIL, PARTIALLY HYDROGENATED

COTTONSEED OIL AND SOYBEAN OILS, MONO AND

DIGLYCERIDES, TBHO AND CITRIC ACID ANTIOXIDANTS

Fig. 3-13

Cholesterol

Testosterone A type of estrogen

Fig. 3-14

THG

Fig. 3-15

MAJOR TYPES OF PROTEINS

Structural Proteins Storage Proteins Contractile Proteins Transport Proteins Enzymes

Fig. 3-15a

Structural Proteins (provide support)

Fig. 3-15b

Storage Proteins (provide amino acids for growth)

Fig. 3-15c

Contractile Proteins (help movement)

Fig. 3-15d

Transport Proteins (help transport substances)

Fig. 3-15e

Enzymes (help chemical reactions)

Fig. 3-16

(a) The general structure of an amino acid

(b) Examples of amino acids with hydrophobic and hydrophilicside groups

Aminogroup

Carboxylgroup

Hydrophobicside group

Hydrophilicside group

Leucine Serine

Sidegroup

Fig. 3-16a

(a) The general structure of an amino acid

Aminogroup

Carboxylgroup

Sidegroup

Fig. 3-16b

(b) Examples of amino acids with hydrophobic and hydrophilicside groups

Hydrophobicside group

Hydrophilicside group

Leucine Serine

Fig. 3-17-1Aminogroup

Carboxylgroup

Sidegroup

Sidegroup

Amino acid Amino acid

Fig. 3-17-2Aminogroup

Carboxylgroup

Sidegroup

Sidegroup

Amino acid Amino acid

Sidegroup

Sidegroup

Dehydration reaction

Peptide bond

Fig. 3-18

Amino acid

1 510

20

15

253035

40

45

50 55

6065

70

75 8085

9095100

105

110 115

120125

129

Fig. 3-19

Normal red blood cell

Sickled red blood cell Sickle-cell hemoglobin

(b) Sickle-cell hemoglobin

(a) Normal hemoglobin

Normal hemoglobin

1 2 3 45 6 7. . . 146

1 2 3 4 5 6 7. . . 146

SE

MS

EM

Fig. 3-19a

Normal red blood cell

(a) Normal hemoglobin

Normal hemoglobin

1 2 3 45 6 7. . . 146

SE

M

Fig. 3-19b

Sickled red blood cell Sickle-cell hemoglobin

(b) Sickle-cell hemoglobin

1 2 3 4 5 6 7. . . 146

SE

M

Fig. 3-20-1

(a) Primarystructure

Fig. 3-20-2

(a) Primarystructure

(b) Secondary structure

Aminoacids

Pleated sheet

Alpha helix

Fig. 3-20-3

(a) Primarystructure

(b) Secondary structure

Aminoacids

Pleated sheet

Alpha helix

(c) Tertiarystructure

Polypeptide

Fig. 3-20-4

(a) Primarystructure

(b) Secondary structure

Aminoacids

Pleated sheet

Alpha helix

(c) Tertiarystructure

Polypeptide

(d) Quaternarystructure

Protein withfour polypeptides

Fig. 3-21

Protein

Target

Fig. 3-22

Gene

DNA

RNA

Protein

Amino acid

Nucleic acids

Fig. 3-23

Nitrogenous base(A, G, C, or T)

Thymine (T)

Phosphategroup

Sugar(deoxyribose)

(a) Atomic structure (b) Symbol used in this book

Phosphate

Base

Sugar

Fig. 3-23a

Nitrogenous base(A, G, C, or T)

Thymine (T)

Phosphategroup

Sugar(deoxyribose)

(a) Atomic structure

Fig. 3-23b

(b) Symbol used in this book

Phosphate

Base

Sugar

Fig. 3-24

Adenine (A) Guanine (G)

Thymine (T) Cytosine (C)

Adenine (A) Guanine (G) Thymine (T) Cytosine (C)

Space-filling model of DNA

Fig. 3-24a

Adenine (A) Guanine (G)

Thymine (T) Cytosine (C)

Fig. 3-24b

Adenine (A) Guanine (G) Thymine (T) Cytosine (C)

Space-filling model of DNA

Fig. 3-25

Sugar-phosphatebackbone

NucleotideBasepair

Hydrogenbond

Bases

(a) DNA strand(polynucleotide)

(b) Double helix(two polynucleotide strands)

Fig. 3-25aSugar-phosphatebackbone

Nucleotide

Bases

(a) DNA strand(polynucleotide)

Fig. 3-25b

Basepair

Hydrogenbond

(b) Double helix(two polynucleotide strands)

Fig. 3-26

Phosphategroup

Nitrogenous base(A, G, C, or U)

Uracil (U)

Sugar (ribose)

Fig. 3-27

DNA

Human cell(DNA in 46

Chromosomes)

Chromosome 2(one DNA molecule)

Section ofchromosome 2

Lactase gene

14,000 nucleotides

C at this site causeslactose intoleranceT at this site causeslactose tolerance

Fig. 3-28

Fig. 3-UN01

Short polymer Monomer Hydrolysis

Dehydrationreaction

Longer polymer

Fig. 3-UN02

Large biologicalmolecules

Functions Components Examples

Carbohydrates

Lipids

Proteins

Nucleic acids

Dietary energy;storage; plantstructure

Long-termenergy storage(fats);hormones(steroids)

Enzymes, structure,storage, contraction,transport, and others

Informationstorage

Monosaccharides:glucose, fructoseDisaccharides:lactose, sucrosePolysaccharides:starch, cellulose

Fats (triglycerides);Steroids(testosterone,estrogen)

Lactase(an enzyme),hemoglobin(a transport protein)

DNA, RNA

Monosaccharide

Components ofa triglyceride

Amino acid

Nucleotide

Fatty acid

Glycerol

Aminogroup

Carboxylgroup

Sidegroup

Phosphate

Base

Sugar

Fig. 3-UN02a

Functions Components Examples

Dietary energy;storage; plantstructure

Monosaccharides:glucose, fructoseDisaccharides:lactose, sucrosePolysaccharides:starch, cellulose

Monosaccharide

Carbohydrates

Fig. 3-UN02b

Functions Components Examples

Lipids

Long-termenergy storage(fats);hormones(steroids)

Fats (triglycerides);Steroids(testosterone,estrogen)Components of

a triglyceride

Fatty acid

Glycerol

Fig. 3-UN02c

Functions Components Examples

Proteins

Enzymes, structure,storage, contraction,transport, and others

Lactase(an enzyme),hemoglobin(a transport protein)

Amino acid

Aminogroup

Carboxylgroup

Sidegroup

Fig. 3-UN02d

Functions Components Examples

Nucleic acids

Informationstorage DNA, RNA

Nucleotide

Phosphate

Base

Sugar

Fig. 3-UN03

Primary structure

(sequence ofamino acids)

Secondary structure

(localized folding)

Tertiary structure

(overall shape)

Quaternary structure

(found in proteins with

multiple polypeptides)

Fig. 3-UN04

DNAdouble helix DNA strand DNA nucleotide

Base

Sugar

Phosphategroup