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chemistry is currently defined as 8. 1.1;1"",11. Some scientists believe that life elsewhere in the
study of compounds made only by living cells. universe might be based on the element silicon, rather than
study of carbon compounds. on carbon, as on Earth. Look at the electron distribution dia
study of vital forces. gram for silicon in Figure 2.9 and draw the Lewis dot struc
study of natural (as opposed to synthetic) compounds. ture for silicon. What properties does silicon share with
study of hydrocarbons. carbon that would make silicon-based life more likely than,
say, neon-based life or aluminum-based life?
of the following hydrocarbons has a double bond in its
skeleton? SCIENTIFIC INQUIRY
9. In 1918, an epidemic of sleeping sickness caused an unusual
rigid paralysis in some survivors, similar to symptoms of ad
vanced Parkinson's disease. Years later, L-dopa (below, left), a
the term that correctly describes the relationship chemical used to treat Parkinson's disease, was given to some
these two sugar molecules: of these patients, as dramatized in the movie Awakenings.
H L-dopa was remarkably effective at eliminating the paralysis, at
I H, 90 least temporarily. However, its
H-C-OH C
I I enantiomer, D-dopa (right),
c=o H-C-OH was subsequently shown to
I I have no effect at all, as is the
H-C-OH H-C-OH
I I case for Parkinson's disease. L-dopa o-dopa
H H
Suggest a hypothesis to explain
c. enantiomers
why, for both diseases, one enantiomer is effective and the
d. isotopes
other is not.
the asymmetric carbon in this molecule:
SCIENCE, TECHNOLOGY, AND SOCIETY
o OHH H H >
subunits
0: helix
25
----------
The primary structure of apr9tem)s . sequence of amino Most proteins have segments of their polypeptide chains
acids. As an exampl~l~ ~~ .n, a globular protein coiled or folded in patterns that contribute to the protein's
found in the blood.~ transports vitamin A and one of the thyroid shape. These coils and folds, collectively referred to as
hormones through9ttt the body. Each of ~~ ~);~dentical polypeptide structure, are the result of hydrogen bonds between the
chains that together~ake uptr~~i);co~ed of 127 amino constituents of the polypeptide backbone (not the amino
acids. Shown here iSt)e!Ofm_cnains unravelettfor a closer look at chains). Both the oxygen and the nitrogen atoms of the
its primary structure. A ~p~~illc one of the 20 ~~ acids, indicated electronegative, \\ith partial negative charges (see Figure
here by its three-letter abbr~villt;/ .f~~~~Ch ofthe 127 positions weakly positive hydrogen atom attached to the nitrogen atom
along the chain. The pro . reiSlike the order of letters in a affinity for the oxygen atom of a nearby peptide bond.
very long word. Ifleft to ~ce, there would be 20 127 different ways these hydrogen bonds are weak, but because they are reJ)eated
of making a polypeptide~in).,27·~9;acids long. However, the times over a relatively long region of the polypeptide chain,
precise primary structure of a'pt~is~aet~ned not by the random support a particular shape for that part of the protein.
linking of amino acids, inherited gene~·lhformation. One such secondary structure is the a helix, a delicate
~~~;7' /.~;:-";;"_,,
*";\ -",j,"
together by hydrogen bonding between every fourth
shown above. Although transthyretin has only one a ""'.lA Il "!'.'VI
tertiary structure), other globular proteins have multiple
a helix separated by nonhelical regions. Some fibrous nrr,t.,ind.
as a-keratin, the structural protein ofhair, have the a helix
over most of their length.
The other main type ofsecondary structure is the ~ l"~;"""""_
As shown above, in this structure two or more regions ofthe
tide chain lying side by side are connected by hydrogen bonds
parts of the two parallel polypeptide backbones. Pleated sheets
up the core ofmany globular proteins. as is the case for tr"'n~tl'.
and dominate some fibrous proteins, including the silk protein
der's web. The teamwork ofso many hydrogen bonds makes
der silk fiber stronger than a steel strand of the same weight.
--- ---
--- ---
on the patterns of secondary structure is a protein's Some proteins consist of two or more polypeptide chains aggre
shown above for the transthyretin polypeptide.
!1rh<'"1"hlr" gated into one functional macromolecule. Quaternary structure is
structure involves interactions between backbone the overall protein structure that results from the aggregation of
tertiary structure is the overall shape of a polypeptide these polypeptide subunits. For example, shown above is the com
from interactions between the side chains (R groups) of the plete, globular transthyretin protein, made up of its four polypep
acids. One type of interaction that contributes to ter tides. Another example is collagen, shown below left, which is a
is-somewhat misleadingly-called a hydrophobic fibrous protein that has helical subunits intertwined into a larger
As a polypeptide folds into its functional shape, amino triple helix, giving the long fibers great strength. This suits collagen
hydrophobic (nonpolar) side chains usually end up in clus fibers to their function as the girders of connective tissue in skin,
core of the protein, out of contact with water. Thus, what bone, tendons, ligaments, and other body parts (collagen accounts
interaction is actually caused by the action of for 40% of the protein in a human body). Hemoglobin, the oxygen
which exclude nonpolar substances as they form binding protein of red blood cells shown below right, is another ex
bonds with each other and with hydrophilic parts of the ample of a globular protein with quaternary structure. It consists of
nonpolar amino acid side chains are close together, four polypeptide subunits, two of one kind ("0'. chains") and two of
interactions help hold them together. Meanwhile, hy another kind ("~ chains"). Both 0'. and ~ subunits consist primarily
between polar side chains and ionic bonds between of O'.-helical secondary structure. Each subunit has a nonpolypep
negatively charged side chains also help stabilize terti
tide component, called heme, with an iron atom that binds oxygen.
These are all weak interactions, but their cumulative
0'. Chains
Hemoglobin
Collagen
walls
EVOLUTION CONNECTION
rgy amylopectin, and cellulose
rgy 10. Comparisons of amino acid sequences can shed light on the
of the following statements concerning unsaturated evolutionary divergence of related species. Would you expect
all the proteins of a given set ofliving species to show the same
,They are more common in animals than in plants.
degree of divergence? Why or why not?
:e
They have double bonds in the carbon chains of their fatty
SCIENTIFIC INQUIRY
generally solidify at room temperature.
contain more hydrogen than saturated fats having 11. During the Napoleonic Wars in the early 1800s, there was a sugar
same number of carbon atoms. shortage in Europe because supply ships could not enter block
have fewer fatty acid molecules per fat molecule. aded harbors. To create artill
100
cial sweeteners, German
level of a protein least affected by a disruption in scientists hydrolyzed wheat
bonding is the starch. They did this by adding
level. d. quaternary leveL hydrochloric acid to heated 50
Dr,'nl'l~rv level. e. All structural levels are starch solutions, breaking
f the following pairs of base sequences could form a between the glucose
o~------------~
sidic linkage in starch using Figures 5.5a and 5.7b for reference.
-IUU"""v with 5' -GCAT-3' Show how the acid was able to break this bond. Why do you
think the add broke only 50% ofthe linkages in the wheat starch?
junctions, desmosomes, and gap junctions. ATP. If a cell is exposed to cyanide, most of the cyanide
... The Cell: A living Unit Greater Than the Sum of Its Parts
a. mitochondria. d. lysosomes.
b. ribosomes. e. endoplasmic
Activity Cell Junctions
c. peroxisomes.
Activity Review: Animal Cell Structure and Function
Activity Review: Plant Cell Structure and Function 9. I.U¥li. From memory, draw two cells, showing the
structures below and any connections between them.