Chapter 5.

THE STRUCTURE AND FUNCTION OF

MACROMOLECULES.
Summary of Chapter 5, BIOLOGY, 9
TH
ED Campbell, by J.B. ee!e et al. "#$$.
Small molecules have unique properties arising from the orderly arrangement of its atoms.
The major groups of biologically important molecules are carbohydrates, lipids, proteins and
nucleic acids.
Usually they are very large containing thousands of atoms: macromolecules.
Macromolecules are giant molecules formed by the union bonding! of smaller molecules.
They consist of hundreds of thousands of atoms. This is another level of biological organi"ation.
POLYMERS
#ost macromolecules are polymers. These are long chains formed by lin$ing small organic
molecules called monomers.
%oly: many& #eros: parts
Polymer!a"on is the lin$ing together of monomers to form polymers. 't ta$es place through
dehydration reactions.
(. Con#ensa"on is the chemical process by )hich monomers are lin$ed together.
* molecule of )ater is removed: #e$y#ra"on syn"$ess.
+ach of the t)o monomers forming the bond contributes one part of the )ater molecule,
the $y#ro%yl &roup ,-./0 and the $y#ro&en ,-/0.
1. Hy#rolyss is the chemical process by )hich polymers can be degraded into monomers.
* molecule of )ater is bro$en into / and ./ and added to the bro$en bonds.
+ach molecular product receives a hydro2yl group or a hydrogen.
/ydrolysis is the reverse of condensation dehydration synthesis!.
* infinite number of polymers can be built from a limited number of monomers.
+ach class of polymer e. g. lipids, proteins, etc.! is formed from a specific set of monomers.
%roteins polymer! are made of thousands of amino acid units monomer!.
The uniqueness of organisms depends on the unique arrangement of the same monomers.
#acromolecules are constructed from only 34 to 54 common monomers and some others that
occur rarely.
CAR'OHYDRATES
Carbohydrates include sugars and their polymers.
Carbohydrates contain carbon hydrogen and o2ygen in a ratio of (:1:( or ,C/1.0n.
Monosacc$ar#es are simple sugars.
They serve as sources of energy and carbon atoms.
5ormally containing 6 to 7 carbon atoms.
* hydro2yl group is bonded to each carbon e2cept one.
That carbon is double bonded to an o2ygen atom forming a car(onyl &roup) depending
on the position of the carbonyl group, the sugar is an aldehyde aldose sugars! or a
$etone $etose sugars!.
8lucose is an aldose and fructose a $etose. #ost sugar names end in %o&e.
Dssacc$ar#es are made of t)o monosaccharide units.
T)o monosaccharide rings joined by a &lycos#c ln*a&e, a covalent bond formed
bet)een t)o monosaccharides by a dehydration reactions.
They can be split by the addition of )ater, hydroly"ed.
#altose is formed by lin$ing t)o glucose monomers and sucrose by lin$ing one glucose
and one fructose. 8lucose lin$ed to galactose produces lactose, the sugar in mil$.
Polysacc$ar#es.
9epeating chains of monosaccharides.
Single long chain or branched chain.
They function either as energy storage material or as building bloc$s of cellular
structures.
ST9UCTU9*: %.:;S*CC/*9'<+S:
Some important polysaccharides:
S"arc$ is made entirely of glucose and is the main storage carbohydrate of plants: (=3
lin$ages& this arrangement ma$es the starch molecule helical.
Amylose is the simplest form of starch& it is unbranched and helical.
Amylopec"n is a branched form )ith (=> lin$ages at the branch point.
Source: http:??))).lsbu.ac.u$?)ater?hysta.html
+lyco&en is made of glucose and is the storage carbohydrate of animals: (=3
lin$ages.
The glycogen molecule contains more branches than the amylopectin molecules.
't is stored mostly in the liver and muscles.
ST9UCTU9*: %.:;S*CC/*9'<+S
Cellulose is also made of glucose monomers and is a structural carbohydrate: (=3
lin$ages.
The angles of the bonds of the (=3 lin$ages ma$e every other glucose monomer
@upside do)n.@
Cellulose molecules are straight and never branched.
'ts hydro2yl groups are free to form hydrogen bonds )ith those of adjacent
molecules.
'n plant cell )alls, cellulose molecules form minute cables called mcro,(rls.
Aery fe) organisms can digest cellulose. 'n most cases cellulose passes through the
digestive tract and is eliminated in the feces.
C$"n is a polysaccharide used by arthropods in building the e2os$eleton.
The chitin monomer is a glucose=li$e molecule called N-ace"yl&lucosamne in )hich
an ./ group is replaced by a chain of 9-5/C.C/6 group.
Bhen it becomes encrusted )ith calcium carbonate, it becomes hard.
Chitin is also found in the cell )all of fungi, insects, spiders, crustaceans and other
animals.
Some modified and comple2 carbohydrates have special roles:
+alac"osamne is a structural carbohydrate present in cartilage& it is amino derivative of
galactose, an enantiomer of glucose.
+lycopro"ens and &lycolp#s are commonly found on the outer surface of cells.
These are proteins )ith polysaccharide or fatty acid branches attached.
LIPIDS
:ipids are diverse group of compounds made mostly of carbon and hydrogen, )ith a fe) o2ygen
atoms found mainly in functional groups.
Hy#rop$o(c molecules: )ater repellent.
They are made mostly of hydrocarbons.
Soluble in nonpolar solvents.
Cor energy storage, hormones, structure of cell membrane.
5eutral fats, phospholipids, steroids, )a2es, carotenoids and other pigments.
S"ora&e lp#s
Cats are large molecules made from smaller molecules lin$ed together by dehydration
reactions.
5eutral fats are made of &lycerol and three ,a""y ac#s.
8lycerol is a 6=carbon alcohol.
Catty acids are long unbranched hydrocarbon chain )ith a carbo2yl group C../! at one end.
The carbon s$eleton of the fatty acid usually has (> to (D carbon atoms.
*t one end there is a carbo2yl group that gives these molecules the name of fatty a!'(&.
The nonpolar C-/ is the reason for the hydrophobic properties of the hydrocarbons.
Bhen a fatty acid combines )ith a glycerol molecule a molecule of )ater is removed and an
es"er ln*a&e is formed.
The fatty acids in a fat molecule may or may not be the same.
Tr&lycer#e triacylglycerol! is a synonym for fat.
Sa"ura"e# ,a"s have a ma2imum number of hydrogen atoms in the chain, and are usually are
solid at room temperature, e. g. lard, blubber and butter.
Unsa"ura"e# ,a"s have double bonds bet)een some of the carbon atoms and have less than
the ma2imum number of hydrogen atoms.
Unsaturated fats have bends in the chains that prevent the aligning )ith the adjacent chain and
prevent the van der Baals forces from acting. They are usually liquid at room temperature, e. g.
vegetable oils.
Cats store at least t)ice as much energy as starch.
/umans and mammals store their fat in the adipose tissue of the body. This tissue serves as a
reservoir of energy, as an insulator, and cushions internal organs.
S"ruc"ural lp#s
P$osp$olp#s are major components of cell membranes.
%hospholipids differ from fats in having only t)o fatty acids instead of three and a phosphate
group )ith a small additional molecule attached to the third carbon of glycerol instead of a
hydro2yl group.
The hydrocarbon chains are hydrophobic but the phosphate group and its attached organic
molecule e. g. choline, lecithin! are hydrophilic affinity for )ater!.
*mphipathic molecule.
%hospholipids form micelles and bilayers or double layers in aqueous solutions.
* mcelle is a droplet formed by phospholipid molecules arranged )ith their hydrophilic
heads facing out to)ard the )ater medium, and their hydrophobic tails facing in)ard
a)ay from the )ater.
'layers are double membranes. 'n a bilayer, the heads face to)ard the aqueous
solution and the tails point to the interior of the membrane.
C$oles"erol is a steroid component of cell membranes of animals.
.a%es are comple2 lipids made of many fatty acids lin$ed to a long=chain alcohol.
/ydrophobic
Coating of fruits and leaves, bees)a2, ear )a2, some insects.
The follo)ing is the simplified structural formula of bees )a2.
http:??))).cyberlipid.org?)a2?)a2444(.htmE1
Func"onal ,a"s
Steroids have their carbon s$eleton bent into four fused rings )ith a carbon chain attached to
one of the rings.
Three rings have si2 carbon atoms and one has five carbons.
There are different functional groups attached to the rings.
The length and structure of the chain distinguishes one steroid from another.
)*ll &tero'(& ha+e the &ame fu,(ame,tal &tru!ture of four -tetra!y!l'!. !arbo, r',/& !alle( the
&tero'( ba!0bo,e or &tero'( ,u!leu&. The a(('t'o, of ('ffere,t !hem'!al /roup& at ('ffere,t
pla!e& o, th'& ba!0bo,e lea(& to the format'o, of ma,y ('ffere,t &tero'(al !ompou,(&, ',!lu(',/
the &e1 hormo,e& pro/e&tero,e a,( te&to&tero,e, the a,t'%',flammatory &tero'( !ort'&o,e, a,(
the !ar('a! &tero'(& ('/o1', a,( ('/'to1',.2 http:??)aynes)ord.palomar.edu?plseptF>.htmEfoam
Some steroids function as hormones e. g. se2 hormones!, chemical messengers in the body of
animals.
The function of steroids depends on the functional groups attached to their carbon rings.
C$oles"erol is a structural component of cell membranes but it is also a precursor from )hich
other steroids are made.
Caro"eno#s are plant pigments involved in photosynthesis. They are insoluble in )ater.
PROTEINS
%roteins ma$e more than 54G of the dry )eight of most cells.
%roteins perform a variety of functions in the body: structural support, transport of other
molecules, body defense, signaling bet)een cells, chemical catalysts called en!ymes, storage,
and other functions. See f'/. 5.$5, pa/e 34.
%roteins vary in their structure so they can perform specific functions.
%roteins are large comple2 molecules, polymers of amino acids, joined by peptide bonds. These
polymers are called polypeptides.
* protein is made one or more polypeptides folded and coiled into a specific conformation.
14 amno ac#s **! involved. See f'/. 5.$5, pa/e 39.
Carbon, hydrogen, o2ygen, nitrogen and usually sulfur.
** contain an amno &roup, 5/1, at one end and a car(o%yl &roup, C../, at the
other end, both attached to an alpha !arbo, H!.
**s have a variable side chain 9 group! that determines the specific physical and
chemical properties of each **.
+2cept for glycine all other (F amino acids used to synthesi"e proteins can e2ist as L= or
D= enantiomorphs. .nly := amino acids are used for protein synthesis.
Iacteria and plants can synthesi"e all **. There are a fe) e2ceptions.
*nimals synthesi"e some but not all **. Essen"al AA must be obtained from the diet.
Summari"ing the four variable components of an amino acid: alpha carbon, amino group,
carbo2yl group and the side chain.
**s are usually ioni"ed in the cell. See 6'/ure 5.$3 o, pa/e 39 of your te1tboo0.
The properties of the ** depend on the side chain.
Non-polar side chain made of hydrocarbons ma$es the ** hydrophobic.
Polar contain ., S or 5 on the side chain ma$ing the **s hydrophilic.
Ne&a"/e side chain ma$es the ** acidic. This is due to the presence of a carbo2yl group in
the side chain that is usually dissociated at the cellular p/.
Pos"/e side chain ma$es the ** basic& the side chains contain amino groups.
Ioth acidic and basic side chains are hydrophilic.
#ore: http:??users.rcn.com?j$imball.ma.ultranet?Iiology%ages?+?+nantiomers.html
Pep"#e (on#
T)o ** combine to form a dipeptide& three form a tripeptide& many form a polypeptide.
The amino end of one ** joins the carbo2yl end of the adjacent **.
*n en"yme cataly"es the dehydration reaction. The resulting covalent bond is called a
pep"#e (on#. See f'/. 5.$3, pa/e 4#.
Bhen this process is repeated thousands of times the resulting molecule is called a
polypep"#e.
%olypeptide chain may contain thousands of **.
%olypeptide and protein are not synonymous.
%roteins consist of one or more polypeptide chains t)isted into a unique shape.
The function of the protein depends on its ability to bind to another molecule.
%roteins have four levels of organi"ation. See f'/. 5."#, pa/e 4" a,( 47.
%rimary structure: a unique se0uence o, AA for each polypeptide chain.
The sequence of ** is determined by inherited genetic information.
*ll proteins of a $ind have the same ** sequence, e. g. all lyso"yme molecules.
* change in the sequence of ** is called a mutation.
Secondary structure results from $y#ro&en (on#s bet)een / and . atoms of the
bac$bone of the chain resulting in coiling 1 $el%! or folding 2 plea"e# s$ee"!. The side
chains atoms are not involved in the secondary structure of polypeptides.
Tertiary structure is the overall shape of the polypeptide due to the interaction among the
s#e c$ans, 9 groups.
Hy#rop$o(c n"erac"ons bet)een side chains usually end up in the interior of the
t)isted polypeptide chain )hile hydrophilic side chains are e2posed to the aqueous
solutions.
Dsul,#e (r#&es are formed bet)een the t)o sulfhydril groups of the ** cysteine.
This is a strong bond.
3an #er .aals ,orces, ionic bonds and hydrogen bonds also contribute to the
tertiary structure of the polypeptide chain.
Juaternary structure is the relationship among several polypeptide chains of a protein.
These polypeptide chains become aggregated into a functional protein.
Cibrous proteins have several polypeptides coiled or aligned into rope=li$e structures.
8lobular proteins are roughly spherical or compact.
The shape of the proteins determines its function.
See animation: http:??))).stolaf.edu?people?giannini?flashanimat?proteins?protein
G14structure.s)f
%rotein conformation depends also on the physical and chemical conditions of the environment
li$e salt concentration, temperature, p/, etc.
Changes in any of these conditions can cause the protein to unravel and become #ena"ure#.
%roteins become #ena"ure# become biologically inactive.
Scientists do not $no) little about the principles of protein folding.
#ost proteins probably go through several intermediate stages before achieving its active
conformation.
C$aperonns or chaperone proteins help in the proper folding of proteins but do not specify the
conformation. They protect the polypeptide from denaturing influences in the cytoplasm.
K=ray crystallography is a method used in determining the three dimensional structure of a
protein.
NUCLEIC ACIDS
+ncoded in the structure of <5* is the information that programs all the cellLs activities.
The <5* molecule contains hundreds of thousands of genes.
+enes determine the polymer sequence of ** in a protein.
%roteins are needed to implement )hat is in the genetic code, in the <5*.
T)o classes: DNA deo2yribonucleic acid! and RNA ribonucleic acid!.
Transmit hereditary information.
<etermine )hat the cells manufacture.
5ucleic acids are polymers that serve blueprints of proteins.
<5* is the genetic material that organisms inherit from their parents.
Flo4 o, &ene"c n,orma"on 4"$n "$e cell.
<5* M m95* M protein
<5* is located in the nucleus of the cell.
%rotein synthesis ta$es place in organelles called ribosomes found in the cytoplasm of the cell.
#essenger 95*, m95*, is synthesi"ed in the nucleus follo)ing the <5* blueprint and then
moves to the ribosomes )ith the message of about the protein to be synthesi"ed.
S"ruc"ure o, nuclec ac#s.
5ucleic acids are polymers of nucleo"#es. They are called polynucleo"#es.
* nucleotide is made of three parts: an organic molecule called a n"ro&enous (ase, a pen"ose
su&ar 5=C sugar!, and a p$osp$a"e &roup.
There are t)o groups of nitrogenous bases: See f'/. 5."5, pa/e 43.
Pyrm#nes5
> member ring of carbon and nitrogen atoms.
5itrogen atoms tend to ta$e /
N
from )ater and from there the name @nitrogenous base@
is derived.
Cytosine C!, thymine T! and uracil U!.
Cytosine is found in both <5* and 95*& thymine is found only in <5*& uracil found only
in 95*.
Purnes5
#ade of a si2=member ring fused to a five=member ring.
5itrogen and carbon ma$e the rings.
*denine *! and guanine 8!.
Ioth are found in <5* and 95*
Pen"ose su&ars:
9ibose is found in 95* and deo2yribose in <5*.
They differ in the absence of an o2ygen atom on the 1=carbon of deo2yribose molecules.
<eo2y= O )ithout an o2ygen.
The combination of a sugar )ith a nitrogenous base forms a nucleos#e )ith an S and not a
T.!
The addition of a phosphate group to a nucleoside ma$es a nucleo"#e also $no)n as a
nucleoside monophosphate.
5ucleotides form polymers )ith the formation of a covalent bond bet)een the phosphate on one
nucleotide and the sugar of the ne2t.
These covalent bond are of a $ind called p$osp$o#es"er (on#.
The resulting polymer forms the bac$bone that )ill ma$e the <5* or 95* molecule. The
nitrogenous bases stic$ out to the side of the bac$bone.
The pentose sugar! in 95* is ribose, and in <5* is deo2yribose.
The carbons in these sugars are numbered and a prime P! after them, e.g. the second
carbon is )ritten as 1Q, t)o prime.
The carbon that stic$ up from the ring is the 5Q carbon.
The phosphodiester lin$ages occur bet)een the -./ group on the 6Q carbon of one nucleotide
and the phosphate on the 5Q of the ne2t.
The t)o free ends of the bac$bone chain are different from each other. .ne end has a
phosphate attached to a 5Q carbon and the other has a hydro2yl attached to 6Q carbon. Be refer
to these as the 5Q and the 6Q ends of the strand.
.nly certain bases are compatible to establish the required hydrogen bonds. 'n other )ords, the
t)o strands of a double heli2 are complementary:
*denine al)ays pairs )ith thymine, a purine )ith a pyrimidine.
8uanine al)ays pairs )ith cytosine.
'f a strands has the sequence *T88C**CC, its complementary strand )ill be T*CC8TT88.
The complementarity of the strands ma$es it possible to ma$e an accurate copy of each of the
t)o strands and, therefore, of the genes.
The linear sequence of bases is passed from parents to offspring. Closely related individuals
have greater similarity in their <5* and proteins than unrelated individuals.
Closely related species )ill share a greater portion of their <5* than distantly related species.
The sequence of nucleotides in these polymers is limitless and so is the number of nitrogenous
bases forming the side branches.
8enes are made of hundreds of nucleotides.
Dou(le $el% an# n$er"ance.
The 95* molecule consists of a single polynucleotide chain.
The <5* molecule is made of t)o polynucleotide chains or strands forming a #ou(le $el%.
The t)o sugar=phosphate bac$bones run in opposite 5QM6Q directions from each other, an
arrangement referred to as an"parallel.
5Q=*T88C**CC=6Q
6Q=T*CC8TT88=5Q
The strands are held together by hydrogen bonds and van der Baals forces established
bet)een facing nitrogenous bases.
Summary of chapter 5 in this site: http:??))).mansfield.ohio=state.edu?Rsabedon?campbl45.htm
(. #acromolecules of life: carbohydrates, lipids, proteins and nucleic acids
1. %olymers and polymeri"ation
#onomers
<ehydration reactions
Condensation reactions
/ydrolysis
6. Carbohydrates
Structure = carbon hydrogen and o2ygen in a ratio of (:1:( or ,C/1.0n.
'nclude sugars and polymers of sugars
#onosaccharides - aldoses and $etoses& ring form in aqueous solutions.
%olysaccharides - glycosidic lin$age
Storage polysaccharides - starch amylose, amylopectin! and glycogen
Structural polysaccharides - cellulose and chitin
3. :ipids
Structure = carbon and hydrogen, )ith a fe) o2ygen atoms found mainly in functional
groups.
/ydrophobic
Cat structure: glycerol, ester lin$age, fatty acids
Catty acid structure - hydrocarbon, carbo2yl group& saturated, unsaturated
%hospholipids - hydrophilic head, hydrophobic tail
Steroids - s$eleton of four fused rings
5. %roteins
Structure - polymer of amino acids
%eptide bond - learn the structure of the peptide bond and ho) it is formed
%olypeptides
Conformation determines ho) it )ords = en"ymes
Cour levels of protein structure
o %rimary: unique sequence of **
o Secondary: repeated portions of coils and folds& alpha heli2, pleated sheets
o Tertiary: formed by the interactions of side chains of the ** that causes three
dimensional structures& ionic and / bonds, disulfide bridges, van der
Baals interactions.
o Juaternary: overall structure of the protein due to the aggregation of several
polypeptide subunits.
Colding and denaturing of proteins
>. 5ucleic *cids
<5* and 95*
%olymers of monomers called nucleotides
5ucleotides structure: sugar, phosphate and nitrogenous base
T)o sugars: ribose and deo2yribose
Cour nitrogenous bases:
o %urines have t)o rings: adenine and guanine
o %yrimidines have one ring: cytosine and thymine or uracil in 95*!
<5* double heli2
Iase pairing: C - 8 and * = T