2009 FIDM/The Fashion Institute of Design & Merchandising

FIDM eLearning Program Page 1 of 3

Chapter 3 The Molecules of Cells

INTRODUCTION TO ORGANIC COMPOUNDS
1. Carbon
a. Next to water, compounds with carbon are the most common substances in
living organisms.
b. Organic compounds = carbon-based molecules
c. Ability to bond with 4 other atoms is basis for building large and diverse
organic compounds
d. Hydrocarbons = contain only carbon and hydrogen
e. Carbon skeleton =a chain of carbon atoms
f. Isomers = compounds with the same formula but different structures
2. Functional groups determine an organic molecules properties, which depend on
the size and shape of the carbon skeleton and the atoms attached to it; all arepolar
which makes them hydrophilic, (water-loving) (see table p. 35)
a. Hydroxyl group
b. Carbonyl group
c. Carboxyl group
d. Amino group
e. Phosphate group
3. Polymers
a. The macromolecules, large biological molecules, are made from smaller
molecular units, called monomers, which are strung together to form long
chains, called polymers.
b. Dehydration reaction = removes a molecule of water to link monomers
together to form polymers
c. Hydrolysis = uses water molecule to break (lyse) apart bonds between
monomers by adding water to them (H- to one monomer, and the OH to
another monomer)

CARBOHYDRATES (hydrophilic)
1. Monosaccharides
a. Monomers - simplest carbohydrates; glucose, fructose
b. Some multiple of CH2O and contains hydroxyl groups and a carbonyl group
c. Disaccharrides = 2 monosaccharides joined together; sucrose, maltose
d. Sweetness - molecules taste sweet because they bind to sweet taste receptors
on the tongue; the shape determines how tightly they bind, and the tighter the
fit the sweeter
2. Polysaccharides
a. Polymers of monosaccharides (mainly glucose)
b. Starch = a glucose polysaccharide; storage molecule in plant roots or tissues
FIDM eLearning Program Page 2 of 3
c. Glycogen = also a glucose polysaccharide; storage of excess sugar in animal
liver and muscle cells
d. Cellulose structural compound (plant cell walls, wood); most abundant organic
compound on Earth; polymer of glucose but in different arrangement, which
prevents most animals from digesting it

LIPIDS (hydrophobic)
1. Diverse compounds composed mostly of carbon and hydrogen atoms linked by
nonpolar covalent bonds makes them hydrophobic (water-fearing)
2. Fat
a. Oil is liquid fat.
b. Energy storage is main function of fat; a gram of fat stores more than twice as
much energy as a gram of starch; fatty tissue also cushions vital organs and
insulates the body
c. Also called triglycerides = consist of three (tri-) fatty acids linked to one
glycerol molecule
d. Unsaturated fats = fatty acids and fats with double bonds cause kinks in the
carbon chain and prevent the bonding of the maximum number of hydrogen
atoms; the kinks prevent molecules from packing tightly together and solidifying
at room temperature; most PLANT fats
e. Saturated fats = fats with the maximum number of hydrogen atoms; most
ANIMAL fats
3. Phospholipids found in cell membranes
4. Waxes more hydrophobic than fats; waxy coats on fruit and insects prevent
dessication (drying out)
5. Steroids cholesterol found in animal cell membranes and other animal cells; used
as starting material for other steroids, including male and female hormones
(testosterone and estrogen); anabolic steroids synthetic variants of testosterone;
too much poses serious health risks

PROTEINS
1. Important to structure and function of cells:
a. enzymes, chemical catalysts that speed and regulate chemical reactions in cells
b. structural proteins in hair, muscle cells
c. defensive proteins antibodies
d. signal proteins hormones and messenger chemicals
e. transport proteins hemoglobin
f. storage proteins egg albumin, plant seeds, milk proteins
2. A protein is a polymer of amino acid monomers linked by peptide bonds forming a
polypeptide; protein diversity is based on the arrangement or different sequences
of the 20 amino acids in the polypeptide
3. Proteins specific shape determines its function: most enzymes and other proteins
are globular in shape; structural proteins are fibrous
4. Protein structure polypeptide chains are folded into unique shapes that determine
the proteins function; 4 structures
a. primary structure specific sequence of amino acids forming its polypeptide
chain
b. secondary structure coiling or folding of the chain, stabilized by hydrogen
bonds
FIDM eLearning Program Page 3 of 3
c. tertiary structure overall three-dimensional shape of the polypeptide,
resulting from the interactions between the R groups
d. quaternary structure - found in proteins made of more than one polypeptide
e. Linus Pauling made important contributions to our understanding of protein
structure and function; associated with controversial belief that large doses of
vitamin C can help prevent colds and other diseases; won Nobel Peace Prize for
helping ban nuclear testing


NUCLEIC ACIDS
1. Polymers that serve as blueprints for proteins: deoxyribonucleic acid (DNA) and
ribonucleic acid (RNA)
2. DNA = genetic material inherited from parents; contain genes that program amino
acid sequences, the primary structure, of proteins, thus controlling the life of the cell
and the organism
3. RNA = information from DNA is transcribed into RNA which is then translated into
the primary structure of proteins
4. Nucleotides = the monomers that make up nucleic acids
a. contains 3 parts: five-carbon sugar, phosphate group, nitrogenous base (4
different bases: guanine (G) , cytosine (C), adenine (A), thymine (T) (in DNA)
or uracil (U) (in RNA); G always pairs with C, and A always pairs with T (U)
b. RNA is a single polynucleotide strand with the sugar ribose.
c. DNA is a double polynucleotide strand with the sugar deoxyribose, twisted into a
double helix with the nitrogenous bases protruding into the center from the two
sugar-phosphate backbones; usually very long molecules with thousands to
millions of base pairs