the chemical building blocks of life chapter 3 adapted by g. cornwall, ph.d. from raven’s biology,...
TRANSCRIPT
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The Chemical BuildingBlocks of Life
Chapter 3
Adapted by G. Cornwall, Ph.D. From Raven’s Biology, McGraw Hill Publishing
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Carbon• Framework of biological
molecules consists primarily of carbon bonded to – Carbon– O, N, S, P or H
• Can form up to 4 covalent bonds• Hydrocarbons – molecule
consisting only of carbon and hydrogen– Nonpolar– Functional groups add chemical
properties
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Isomers• Molecules with the same
molecular or empirical formula– Structural isomers– Stereoisomers – differ in
how groups attached• Enantiomers
– mirror image molecules– chiral– D-sugars and L-amino
acids
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Macromolecules• Polymer – built by linking
monomers• Monomer – small,
similar chemical subunits
• Three things to keep track of in all four macromolecules– What is the Monomer – What is the Polymer– What is Bond
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• Dehydration synthesis– Formation of large molecules by the removal of water– Monomers are joined to form polymers
• Hydrolysis– Breakdown of large molecules by the addition of
water– Polymers are broken down to monomers
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Carbohydrates
• Molecules with a 1:2:1 ratio of carbon, hydrogen, oxygen
• Empirical formula (CH2O)n
• C—H covalent bonds hold much energy– Carbohydrates are good energy storage
molecules– Examples: sugars, starch, glucose
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Monosaccharides
• Simplest carbohydrate• 6 carbon sugars play important roles
• Glucose C6H12O6
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• Fructose is a structural isomer of glucose• Galactose is a stereoisomer of glucose• Enzymes that act on different sugars can
distinguish structural and stereoisomers of this basic six-carbon skeleton
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Disaccharides
• 2 monosaccharides linked together by dehydration synthesis
• Used for sugar transport or energy storage
• Examples: sucrose, lactose, maltose
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Polysaccharides• Long chains of monosaccharides
– Linked through dehydration synthesis
• Energy storage– Plants use starch– Animals use glycogen
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Polysaccharides
• Structural support– Plants use cellulose– Arthropods and fungi use chitin
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Nucleic acids
• Polymer – nucleic acids• Monomers – nucleotides
– sugar + phosphate + nitrogenous base
– sugar is deoxyribose in DNA or ribose in RNA
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– Nitrogenous bases include• Purines: adenine and guanine• Pyrimidines: thymine, cytosine, uracil
– Nucleotides connected by phosphodiester bonds
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Deoxyribonucleic acid (DNA)• Encodes information for
amino acid sequence of proteins– Sequence of bases
• Double helix – 2 polynucleotide strands connected by hydrogen bonds– Base-pairing rules
• A with T (or U in RNA)• C with G
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Ribonucleic acid (RNA)
• RNA similar to DNA except– Contains ribose instead of
deoxyribose– Contains uracil instead of
thymine
• Single polynucleotide strand
• RNA uses information in DNA to specify sequence of amino acids in proteins
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Other nucleotides
• ATP adenosine triphosphate– Primary energy currency of the cell
• NAD+ and FAD+
– Electron carriers for many cellular reactions
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Card Quiz A
The addition of water to break a chemical bond is termed –
Dehydration synthesis Hydrolysis Condensation Disassociation
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Card Quiz A
The monomers of DNA are covalently bonded together. These bonds are called phosphodiester bonds.
This is true This is false
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Card Quiz A
Which of the following is not part of a nucleotide? 5 carbon sugar Phosphate group Fatty acid chain Nitrogenous base
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Card Quiz A
Dehydration synthesis – Is used to link monomers Removes water to form bonds Is involved in protein synthesis All of the above
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Card Quiz A
If a strand of DNA has a sequence ATCCTAG, what would be the complementary sequence?
CGAAGAT TAGGATC TACCGGA CGAAGTC
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Card Quiz Answers
Blue Green Red
Yellow Red
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ProteinsProtein functions include:
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• Proteins are polymers– Composed of 1 or more long, unbranched chains– Each chain is a polypeptide
• Amino acids are monomers• Amino acid structure
– Central carbon atom– Amino group– Carboxyl group– Single hydrogen– Variable R group
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• Amino acids joined by dehydration synthesis– Peptide bond
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• Polypeptide chains fold in various ways to form the final 3-D shape
• The shape of a protein determines its function
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4 Levels of protein structure1. Primary structure – sequence of amino
acids (beads on a string)
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1. Secondary structure – interaction of groups in the peptide backbone helix sheet
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3. Tertiary structure – final folded shape of a globular protein
– Stabilized by a number of forces– Final level of structure for proteins consisting
of only a single polypeptide chain
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4. Quaternary structure – arrangement of individual chains (subunits) in a protein with 2 or more polypeptide chains
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Additional structural characteristics
• Motifs – Common elements of secondary structure
seen in many polypeptides– Useful in determining the function of unknown
proteins
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• Domains– Functional units within a larger structure– Most proteins made of multiple domains that
perform different parts of the protein’s function
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• Once thought newly made proteins folded spontaneously
• Chaperone proteins help protein fold correctly
• Deficiencies in chaperone proteins implicated in certain diseases– Cystic fibrosis is a hereditary disorder
• In some individuals, protein appears to have correct amino acid sequence but fails to fold
Chaperones
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Denaturation
• Protein loses structure and function
• Due to environmental conditions– pH– Temperature– Ionic concentration of
solution
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Lipids
• Loosely defined group of molecules with one main chemical characteristic– They are insoluble in water
• High proportion of nonpolar C—H bonds causes the molecule to be hydrophobic
• Fats, oils, waxes, and even some vitamins
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Fats• Triglycerides
– Composed of 1 glycerol and 3 fatty acids
• Fatty acids – Need not be identical– Chain length varies– Saturated – no double bonds between carbon
atoms• Higher melting point, animal origin
– Unsaturated – 1 or more double bonds• Low melting point, plant origin
– Trans fats produced industrially
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Phospholipids• Composed of
– Glycerol– 2 fatty acids – nonpolar “tails”– A phosphate group – polar “head”
• Form all biological membranes
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• Micelles – lipid molecules orient with polar (hydrophilic) head toward water and nonpolar (hydrophobic) tails away from water
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• Phospholipid bilayer – more complicated structure where 2 layers form– Hydrophilic heads point outward– Hydrophobic tails point inward toward each
other
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Other Kinds of Lipids
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Card Quiz B
What is the function of chaperonin proteins? Denaturation of polypeptides Assembling amino acids Regulation of gene expression Folding proteins
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Card Quiz B
Which lipid forms membranes? Triglycerides Steroids Phospholipids Terpenes
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Card Quiz B
Which of the following is not a function of proteins? Catalyzes chemical reactions Transport of material Structural components of tissues All of the above are protein functions
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Card Quiz B
Which of the following is an amino group? -OH -C=O -COOH -NH2
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Card Quiz B
Lincosamides are a class of antibiotics that inhibit peptide bond formation. What type of biological molecule would be effected?
Lipids Proteins Nucleic Acids Carbohydrates
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Card Quiz B
What happens when a lipid is hydrogenated? Hydrogen is added to the fatty acid chains The melting point is raised The lipid is converted into a saturated fat The fatty acid chain is straightened All of the above
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Card Quiz Answers
Yellow Red
Yellow Red
Yellow Green