Chapter 3 The Chemical Building Blocks of Life

Four categories of biological macromolecules: carbohydrates proteins nucleic acids lipids

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Biological molecules consist primarily of

carbon bonded to carbon, or carbon bonded to other atoms

carbon can form up to 4 covalent bonds carbon may be bonded to functional groups with specific properties, for example

Biological molecules are typically large molecules (macromolecules) constructed from smaller subunits monomer: single subunit (mono = 1; -mer = unit) polymer: many units (poly = many) proteins: polymers of amino acids lipids: polymers of fatty acids nucleic acids: polymers of nucleotides complex carbs: polymers of monosaccharides

dehydration synthesis: formation of macromolecules by the removal of water monomers are joined to form polymers hydrolysis: breakdown of macromolecules by the addition of water polymers are broken down to monomers

Fig. 3.4
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Carbohydrates 1:2:1 ratio of carbon, hydrogen, oxygen

empirical formula: (CH2O)n

examples: sugars, starch, glucose

good energy storage molecules C H covalent bonds hold much energy

Fig. 3.5
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Glucose

a monosaccharide containing 6 carbons very important in energy storage fructose is a structural isomer of glucose galactose is a stereoisomer of glucose C6H12O6 or (CH2O)6

Glucose
forms six-membered ring structure in solution can result in two forms

Disaccharides
2 monosaccharides linked together by dehydration synthesis used for sugar transport or energy storage examples: sucrose, lactose, maltose

sucrose (table sugar): -glucose + fructose lactose? maltose?

Polysaccharides: long chains of sugars used for energy storage

plants use starch; animals use glycogen

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Polysaccharides: used for structural support

plants use cellulose some animals use chitin

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Nucleic Acids
two types: DNA and RNA
specialized for the storage, transmission, and use of genetic information

polymers of nucleotides
nucleotides = sugar + phosphate + nitrogenous base deoxyribose in DNA ribose in RNA

Note which carbons of the sugar moiety have the hydroxyl and phosphate groups attached
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Nitrogenous bases:
purines: adenine and guanine pyrimidines: thymine, cytosine, uracil
DNA= Adenine Guanine Cytosine Thymine RNA= Adenine Guanine Cytosine Uracil

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DNA
nucleotides connected by phosphodiester bonds double helix: the two polynucleotide strands connected by hydrogen bonds polynucleotide strands are complementary genetic information is carried in the sequence of nucleotides

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RNA
contains ribose instead of deoxyribose contains uracil instead of thymine single polynucleotide strand functions: read the genetic information in DNA direct the synthesis of proteins

Fig. 3.16
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Other important nucleotide molecules NAD+ and FAD

electron carriers for many cellular reactions

ATP: adenosine triphosphate

primary energy currency of the cell

ATP adenine 5-C sugar (which one?) 3 phosphate groups

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Every function of life involves PROTEINs

Functions include: 1. enzyme catalysts 2. defense 3. transport 4. support 5. motion 6. regulation 7. storage

See Table 3.2 The Many Functions of Protein

You use protein to: think store energy move grow release energy >skin, hair, blood, etc. digest reproduce breathe die

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Proteins are polymers of AMINO ACIDS

The R group is what gives each amino acid its characteristics

General structure of an amino acid

R H N H
amino group

C C H

OH O
carboxyl group
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R group structure dictates the chemical properties of the aa

aas can be classified as: 6 nonpolar (-CH2 or CH3) 6 are polar uncharged (oxygen or OH) 5 charged (acids or bases that can ionize) aromatic (carbon rings) special function Pro kinks (bends) Met first aa in protein Cys links chains
Fig. 3.20 p. 47
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Proteins are polymers of amino acids

joined by dehydration synthesis peptide bonds form between adjacent amino acids
proteins can be small: peptides (up to ~ 50 aas) polypeptides (up to thousands of aas long) proteins get their shape from the order of aas and the R groups on those aas with 20 aas, you can put them together in a combination to do almost anything.

Fig. 3.19

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A proteins function depends on its shape

its shape depends on the sequence of amino acids Primary structure: the sequence of amino acids Secondary structure: local folding of the chain into common shapes

Fig. 3.22

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Tertiary structure: one completely folded chain Quaternary structure: more than one completely folded chain

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Interactions that contribute to a proteins shape!

Fig. 3.21

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Motifs
common elements of 2 structure seen in many polypeptides

Domains
functional regions of a polypeptide result of 3 structure

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Protein folding is aided by chaperone proteins

example from E. coli: GroE chaperonins

Some diseases result from improper folding: cystic fibrosis possibility in Alzheimers disease

Fig. 3.24

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Denaturation = change in the shape of a protein

causing loss of function may involve complete unfolding caused by changes in the proteins environment
pH temperature salt concentration

Fig. 3.25

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Lipids
group of molecules that are insoluble in water
high proportion of nonpolar CH bonds causes the molecule to be hydrophobic

two main categories:

fats (triglycerides) phospholipids

functions:
fuel storage insulation biological barriers biological signals
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Triglycerides (fats)
composed of 1 glycerol + 3 fatty acids

Fatty acids
long hydrocarbon chains which may be

saturated
solid at room temperature most animal fats

unsaturated / polyunsaturated
liquid at room temperature plant fats (oils)

Fig. 3.27

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The shape of the chain affects melting point

saturated: FA chain has the maximum Hs possible unsaturated: presence of double bonds (not H-saturated) polyunsaturated: more than one double bond

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Other Lipids

Fig. 3.28

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Phospholipids contain polar heads and nonpolar tails

composed of: 1 glycerol 2 fatty acids a phosphate group

Fig. 3.29
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Phospholipids spontaneously form micelles or lipid bilayers hydrophobic regions of the phospholipid toward the inside hydrophilic regions exposed to the water environment lipid bilayers are the basis of biological membranes

Fig. 3.30

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Chapter 3 Bonus Topics chiral molecules (enantiomers) renaturation of RNase

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