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Dehydration removes a water molecule, forming a new bond H2O

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1 Dehydration removes a water molecule, forming a new bond H2O
Fig. 5-2a HO 1 2 3 H HO H Short polymer Unlinked monomer Dehydration removes a water molecule, forming a new bond H2O HO 1 2 3 4 H Longer polymer (a) Dehydration reaction in the synthesis of a polymer

2 HO 1 2 3 4 H H2O HO 1 2 3 H HO H (b) Hydrolysis adds a water
Fig. 5-2b HO 1 2 3 4 H Hydrolysis adds a water molecule, breaking a bond H2O HO 1 2 3 H HO H (b) Hydrolysis of a polymer

3 Aldoses Glyceraldehyde Ribose Glucose Galactose Ketoses
Fig. 5-3 Trioses (C3H6O3) Pentoses (C5H10O5) Hexoses (C6H12O6) Aldoses Glyceraldehyde Ribose Glucose Galactose Ketoses Dihydroxyacetone Ribulose Fructose

4 Pentane 2-methyl butane (a) Structural isomers
cis isomer: The two Xs are on the same side. trans isomer: The two Xs are on opposite sides. (b) Geometric isomers L isomer D isomer (c) Enantiomers

5 Effective Enantiomer Ineffective Enantiomer Drug Condition Pain; inflammation Ibuprofen S-Ibuprofen R-Ibuprofen Albuterol Asthma R-Albuterol S-Albuterol

6 (a) Linear and ring forms (b) Abbreviated ring structure
Fig. 5-4 (a) Linear and ring forms (b) Abbreviated ring structure

7 (a) Dehydration reaction in the synthesis of maltose
Fig. 5-5 1–4 glycosidic linkage Glucose Glucose Maltose (a) Dehydration reaction in the synthesis of maltose 1–2 glycosidic linkage Glucose Fructose Sucrose (b) Dehydration reaction in the synthesis of sucrose

8 (a) Starch: a plant polysaccharide
Fig. 5-6 Chloroplast Starch Mitochondria Glycogen granules 0.5 µm 1 µm Amylose Glycogen Amylopectin (a) Starch: a plant polysaccharide (b) Glycogen: an animal polysaccharide

9 (b) Starch: 1–4 linkage of  glucose monomers
Fig. 5-7bc (b) Starch: 1–4 linkage of  glucose monomers (c) Cellulose: 1–4 linkage of  glucose monomers

10 Cell walls Cellulose microfibrils in a plant cell wall Microfibril
Fig. 5-8 Cell walls Cellulose microfibrils in a plant cell wall Microfibril 10 µm 0.5 µm Cellulose molecules Glucose monomer

11 (a) The structure of the chitin monomer. (b) (c) Chitin forms the
Fig. 5-10 (a) The structure of the chitin monomer. (b) Chitin forms the exoskeleton of arthropods. (c) Chitin is used to make a strong and flexible surgical thread.

12 Fatty acid (palmitic acid) Glycerol
Fig. 5-11a Fatty acid (palmitic acid) Glycerol (a) Dehydration reaction in the synthesis of a fat

13 Fat molecule (triacylglycerol)
Fig. 5-11b Ester linkage (b) Fat molecule (triacylglycerol)

14 Structural formula of a saturated fat molecule Stearic acid, a
Fig. 5-12a Structural formula of a saturated fat molecule Stearic acid, a saturated fatty acid (a) Saturated fat

15 unsaturated fatty acid Oleic acid, an cis double bond causes bending
Fig. 5-12b Structural formula of an unsaturated fat molecule Oleic acid, an unsaturated fatty acid cis double bond causes bending (b) Unsaturated fat

16 Choline Hydrophilic head Phosphate Glycerol Fatty acids
Fig. 5-13 Choline Hydrophilic head Phosphate Glycerol Fatty acids Hydrophobic tails Hydrophilic head Hydrophobic tails (a) Structural formula (b) Space-filling model (c) Phospholipid symbol

17 Fig. 5-14 Hydrophilic head WATER Hydrophobic tail WATER

18 Fig. 5-15

19 Table 5-1

20 Fig. 5-UN1  carbon Amino group Carboxyl group

21 Fig. 5-17 Nonpolar Glycine (Gly or G) Alanine (Ala or A) Valine
(Val or V) Leucine (Leu or L) Isoleucine (Ile or I) Methionine (Met or M) Phenylalanine (Phe or F) Trypotphan (Trp or W) Proline (Pro or P) Polar Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q) Electrically charged Acidic Basic Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H)

22 Amino end (N-terminus) Carboxyl end (C-terminus)
Fig. 5-18 Peptide bond (a) Side chains Peptide bond Backbone Amino end (N-terminus) Carboxyl end (C-terminus) (b)

23 Fig. 5-21 Primary Structure Secondary Structure Tertiary Structure
Quaternary Structure  pleated sheet +H3N Amino end Examples of amino acid subunits  helix

24 +H3N Primary Structure Amino end Amino acid subunits 1 5 10 15 20 25
Fig. 5-21a Primary Structure 1 5 +H3N Amino end 10 Amino acid subunits 15 20 25

25 Fig. 5-21b +H3N Amino end Amino acid subunits Carboxyl end 1 5 10 15
20 25 75 80 85 90 95 105 100 110 115 120 125 Carboxyl end

26 Secondary Structure  pleated sheet Examples of amino acid subunits
Fig. 5-21c Secondary Structure  pleated sheet Examples of amino acid subunits  helix

27 Abdominal glands of the spider secrete silk fibers
Fig. 5-21d Abdominal glands of the spider secrete silk fibers made of a structural protein containing  pleated sheets. The radiating strands, made of dry silk fibers, maintain the shape of the web. The spiral strands (capture strands) are elastic, stretching in response to wind, rain, and the touch of insects.

28 Tertiary Structure Quaternary Structure
Fig. 5-21e Tertiary Structure Quaternary Structure

29 Hydrophobic interactions and van der Waals interactions Polypeptide
Fig. 5-21f Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Disulfide bridge Ionic bond

30 Polypeptide  Chains chain Iron Heme  Chains Hemoglobin Collagen
Fig. 5-21g Polypeptide chain  Chains Iron Heme  Chains Hemoglobin Collagen

31 Fig. 5-22 Normal hemoglobin Sickle-cell hemoglobin Primary structure
Val His Leu Thr Pro Glu Glu Val His Leu Thr Pro Val Glu 1 2 3 4 5 6 7 1 2 3 4 5 6 7 Exposed hydrophobic region Secondary and tertiary structures Secondary and tertiary structures  subunit  subunit Quaternary structure Normal hemoglobin (top view) Quaternary structure Sickle-cell hemoglobin Function Molecules do not associate with one another; each carries oxygen. Function Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced. 10 µm 10 µm Red blood cell shape Normal red blood cells are full of individual hemoglobin moledules, each carrying oxygen. Red blood cell shape Fibers of abnormal hemoglobin deform red blood cell into sickle shape.

32 Fig. 5-23 Denaturation Normal protein Denatured protein Renaturation

33 DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM
Fig DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM

34 DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2
Fig DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm via nuclear pore

35 DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2
Fig DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm via nuclear pore Ribosome 3 Synthesis of protein Amino acids Polypeptide

36 (a) Polynucleotide, or nucleic acid (c) Nucleoside components: sugars
Fig. 5-27 5 end Nitrogenous bases Pyrimidines 5C 3C Nucleoside Nitrogenous base Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Purines Phosphate group Sugar (pentose) 5C Adenine (A) Guanine (G) 3C (b) Nucleotide Sugars 3 end (a) Polynucleotide, or nucleic acid Deoxyribose (in DNA) Ribose (in RNA) (c) Nucleoside components: sugars

37 (c) Nucleoside components: nitrogenous bases
Fig. 5-27c-1 Nitrogenous bases Pyrimidines Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Purines Adenine (A) Guanine (G) (c) Nucleoside components: nitrogenous bases

38 (c) Nucleoside components: sugars
Fig. 5-27c-2 Sugars Deoxyribose (in DNA) Ribose (in RNA) (c) Nucleoside components: sugars

39 5' end 3' end Sugar-phosphate backbones Base pair (joined by
Fig. 5-28 5' end 3' end Sugar-phosphate backbones Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand 3' end 5' end New strands 5' end 3' end 5' end 3' end

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