Matriculation Biology - Molecule of Life

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com
TOPIC 1 : MOLECULES OF LIFE
Retold by,
Amran Md Said
Matriculation College of Pahang
SUBTOPIC :
! "ater
!# Carbohydrate$
!% &i'id$
!( Protein
!) *ucleic acid$
1.1 WATER
At the end of thi$ to'ic, $tudent$ $hould be able to:
e+'lain the $tructure of ,ater molecule
de$cribe the 'ro'ertie$ of ,ater and it$ im'ortance
Structure of a ,ater molecule
A ,ater molecule con$i$t of an o+ygen atom and t,o hydrogen atom$
The t,o hydrogen atom$ are combined ,ith the o+ygen atom by $haring of electron$
The three atom$ form a triangle, not a $traight line
The ,ater molecule i$ electrically neutral but there i$ a net negati-e charge on the
o+ygen atom and a net 'o$iti-e charge on both hydrogen atom$!
A molecule carrying $uch an une.ual di$tribution of electrical charge i$ called a 'olar
molecule!
The 'o$iti-ely charged hydrogen atom$ of one ,ater molecule are attracted to the
negati-ely charged o+ygen atom$ of nearby ,ater molecule$ by force$ called hydrogen
bond$!
Http://matriculation-biology.blogspot.com
/ydrogen bond$ largely account for the uni.ue 'ro'ertie$ of ,ater! ,ea0er than
co-alent bond$!
But 12 $trong enough to hold ,ater molecule$ together!
Becau$e of their hydrogen bond$, ,ater molecule$ are attracted to charged 'article$ or
charged $urface$!
Pro'ertie$ of ,ater a$ -ital con$tituent of life
1. Water as a universal solvent
'o,erful $ol-ent for 'olar $ub$tance$!
The$e include ionic $ub$tance$ li0e $odium chloride 3*a
4
and Cl
1
5, and al$o organic
molecule$ ,ith ioni6ed
The$e cation$ 3negati-ely charged ion$5 and anion$ 3'o$iti-ely charged ion$5 become
$urrounded by a $hell of orientated ,ater molecule$!
Thi$ ma0e$ them more reacti-e chemically than ,hen they form 'art of an undi$$ol-e
$olid!
At the $ame time, non1'olar $ub$tance$ are re'elled by ,ater, a$ in the ca$e of oil on
the $urface of ,ater! *on1'olar $ub$tance$ are hydro'hobic!
2. Low visosit! o" water
Thi$ uni.ue 'ro'erty ma0e$ it $uitable medium of tran$'ortation in li-ing organi$m$!
/el'$ in mo-ement of food $ub$tance$
It al$o can act a$ a lubricant$ in 7oint$
#. $i%& s'ei"i &eat a'ait!
A lot of energy i$ re.uired to rai$e the tem'erature of ,ater!
Becau$e, much energy i$ needed to brea0 the hydrogen bond$ !
The head ca'acity of ,ater i$ the amount of head re.uired to rai$e the tem'erature of
g of ,ater by
o
C 'er calorie 3cal5 or cal8g of ,ater 'er
o
C
Thi$ 'ro'erty of ,ater i$ 0no,n a$ it$ high $'ecific heat ca'acity!
The $'ecific heat ca'acity of ,ater i$ the highe$t of any 0no,n $ub$tance!
A.uatic en-ironment$ li0e $tream , la0e$ and $ea$ are all -ery $lo, to change
tem'erature ,hen the $urrounding air tem'erature change$!
(. Latent &eat o" va'ori)ation o" water
"hen 'ure ,ater i$ heated to 99
o
C, it boil$
The ,ater molecule$ gain $ufficient 0inetic energy to e$ca'e into the air a$ ,ater -a'or
The heat energy that i$ being u$ed to 'roduce thi$ change i$ called the latent heat of
-a'ori6ation
"ater ha$ a high latent heat of -a'ori6ation
Becau$e : the hydrogen bond$ bet,een ,ater molecule$ ma0e it difficult for them to
be $e'arated and -a'ori6ed
Thi$ mean$ that much energy i$ needed to turn li.uid ,ater into ,ater -a'or!
The amount of heat energy needed to melt ice i$ -ery high and the amount of heat that
mu$t be remo-ed from ,ater to turn into ice i$ al$o great!
Many li-ing organi$m u$e thi$ feature of ,ater a$ cooling mechani$m!
;or e+am'le, human $,eat : the li.uid ,ater in $,eat ab$orb$ heat energy from the
$0in or in tran$'iration from green lea-e$ : to $to' the lea-e$< tem'erature from ri$ing
too high on a hot day
*. E""et o" te+'erature on water ,ensit!
Mo$t li.uid$ contract on cooling, reaching their ma+imum den$ity at their free6ing 'oint!
"ater i$ unu$ually reaching it$ ma+imum den$ity at (=C!
A$ ,ater free6e$, the ice formed i$ le$$ den$e than the cold A$ ,ater free6e$, the ice formed i$ le$$ den$e than the cold ,ater around it! The ice ,ater around it! The ice
float$ on to'! float$ on to'!
The floating layer of ice in$ulate$ the ,ater belo,! The floating layer of ice in$ulate$ the ,ater belo,!
Thi$ i$ ,hy the bul0 of 'ond$, la0e$ or the $ea rarely free6e $olid!
A.uatic life can generally $ur-i-e a free6e1u'!
-. $i%& Sur"ae Tension . a,&esive an, o&esive "ores
"ater adhere$ $trongly to mo$t $urface$
It can be dro,n u' into long column$ through narro, tube$ li0e the +ylem -e$$el$ of
'lant $tem$, ,ithout the ,ater column brea0ing!
Com'ared ,ith other li.uid$, ,ater ha$ e+tremely $trong adhe$i-e and cohe$i-e
'ro'ertie$ that 're-ent the column brea0ing under ten$ion!
The outermo$t molecule$ of ,ater form hydrogen bond$ ,ith ,ater molecule$ belo,
them!
Thi$ gi-e$ a -ery high $urface ten$ion to ,ater1 higher than that of any other li.uid
e+ce't mercury! Surface $0ate!
The in$ect<$ ,a+y cuticle 're-ent$ ,etting of it$ body, and the ma$$ of the in$ect i$ not
great enough to brea0 through the $urface!
!# CARBO/>?RAT@S
&earning Outcome$:
At the end of the le$$on, $tudent $hould be able to e+'lain:
! ?e$cribe -ariou$ form$ and cla$$e$
#! ?e$cribe the formation and brea0do,n of malto$e
%! Structure$ and function$ of $tarch, glycogen and cellulo$e!
Intro,ution
Organic molecule containing the element carbon, hydrogen and o+ygen in a :#: ratio Organic molecule containing the element carbon, hydrogen and o+ygen in a :#: ratio
"ritten a$ 3C/ "ritten a$ 3C/
# #
O5 O5
n n
A n B number of carbon A n B number of carbon
U$e of carbohydrate$: U$e of carbohydrate$:
Soure o" ener%! Soure o" ener%!
Stora%e o" ener%! Stora%e o" ener%!
Strutural o+'onent o" ell +e+/ranes an, ell walls Strutural o+'onent o" ell +e+/ranes an, ell walls
Carbohydrate$ can be cla$$ified into three cla$$e$: Carbohydrate$ can be cla$$ified into three cla$$e$:
! mono$accharide$ :1 $ingle $ugar$ ! mono$accharide$ :1 $ingle $ugar$
#! di$accharide$ :1 double $ugar$ #! di$accharide$ :1 double $ugar$
%! 'oly$accharide$ :1 many $ugar$ %! 'oly$accharide$ :1 many $ugar$
MO0OSACC$ARI1ES
P&!sial C&arateristi:
1. S+all
2. W&ite
#. Sweet
(. Solu/le
*. Can /e r!stalli)e,
C&e+istr! C&arateristi
1. re,uin% 2ene,it test
2. on,ensation reation to "or+ ,isa&ari,e or 'ol!sa&ari,e
Cree0 ,ord$, monos B $im'leA sacchar B $ugar, generally ha-e molecular formula that
are $ome multi'le of C/
#
O!
1 3C/#O5n 3C/#O5n ;or e+am'le, gluco$e ha$ the formula C
D
/
#
O
D
!
Mo$t name$ for $ugar$ end in 1ose.
ba$ic unit or monomer unit or monomer
It can be cla$$ified by t,o ,ay$ : It can be cla$$ified by t,o ,ay$ :
! ! By the number of carbon$ in the bac0bone By the number of carbon$ in the bac0bone
#! #! By the functional grou' By the functional grou'
Cla$$ification by the number of carbon in the bac0bone Cla$$ification by the number of carbon in the bac0bone
Three carbon 3%C5 E trio$e $ugar$ ! @+am'le : gly$eraldehyde and dihydro+yaceton Three carbon 3%C5 E trio$e $ugar$ ! @+am'le : gly$eraldehyde and dihydro+yaceton
;i-e carbon 3)C5 E 'ento$e $ugar$! @+am'le : ribo$e and ribulo$e ;i-e carbon 3)C5 E 'ento$e $ugar$! @+am'le : ribo$e and ribulo$e
Si+ carbon 3D5 E he+o$e $ugar$ @+am'le : gluco$e and fructo$e Si+ carbon 3D5 E he+o$e $ugar$ @+am'le : gluco$e and fructo$e
Ring Structure for 'ento$e
Im'ortance a$ $ynthe$i$ of nucleic acid 3R*A and ?*A5
Ring Structure for he+o$e
Im'ortance a$ $ource of energy in cell re$'iration
Cla$$ification by the functional grou' Cla$$ification by the functional grou'
@+am'le : @+am'le :
Aldehyde grou' E gly$eraldehyde, ribo$e and gluco$e Aldehyde grou' E gly$eraldehyde, ribo$e and gluco$e
Fetone grou' E dihydro+yaceton, ribulo$e and fructo$e Fetone grou' E dihydro+yaceton, ribulo$e and fructo$e
;unctional Crou'$
?ifference$ bet,een aldehyde and 0etone grou' ?ifference$ bet,een aldehyde and 0etone grou'
All $ugar contain the C B O! Thi$ i$ called a carbonyl grou' All $ugar contain the C B O! Thi$ i$ called a carbonyl grou'
The mono$accharide$ ,hich ha-e a aldehyde grou' i$ called aldo$e $ugar The mono$accharide$ ,hich ha-e a aldehyde grou' i$ called aldo$e $ugar
The mono$accharide$ ,hich ha-e 0etone grou' i$ called 0eto$e $ugar The mono$accharide$ ,hich ha-e 0etone grou' i$ called 0eto$e $ugar
Carbonyl Crou'$ Carbonyl Crou'$
If the location of carbonyl grou' i$ in the middle bac0bone of the corbon, it call 0eto$e If the location of carbonyl grou' i$ in the middle bac0bone of the corbon, it call 0eto$e
Reducing $ugar Reducing $ugar
Aldehyde$ are reducing agent$! Aldehyde$ are reducing agent$!
So aldo$e $ugar ha-e reducing agent$, and are called reducing $ugar! So aldo$e $ugar ha-e reducing agent$, and are called reducing $ugar!
Feto$e $ugar$ do not ha-e reducing agent$, but in mono$accride form, it react a$ Feto$e $ugar$ do not ha-e reducing agent$, but in mono$accride form, it react a$
reducing agent$ becau$e hydro+yl in functional grou' ha-e free! reducing agent$ becau$e hydro+yl in functional grou' ha-e free!
Benedict<$ te$t Benedict<$ te$t
Benedict<$ reagent contain$ co''er 3II5 ion$, ,hich gi-e a blue colour to the Benedict<$ Benedict<$ reagent contain$ co''er 3II5 ion$, ,hich gi-e a blue colour to the Benedict<$
$olution! $olution!
"hen heated ,ith a reducing $ugar, the co''er 3II5 ion$ are reduced to co''er 3I5 ion$, "hen heated ,ith a reducing $ugar, the co''er 3II5 ion$ are reduced to co''er 3I5 ion$,
and an orange1red 'reci'itate of co''er 3I5 o+ide i$ formed: and an orange1red 'reci'itate of co''er 3I5 o+ide i$ formed:
reducing 4 Cu reducing 4 Cu
#4 #4
: : o+idi$ed 4 Cu o+idi$ed 4 Cu
4 4
$ugar 3o+idi$ed5 $ugar 3reduced5 $ugar 3o+idi$ed5 $ugar 3reduced5
ISOM@R ISOM@R
I$omer B molecule$ ,hich ha-e $ame chemical formula but I$omer B molecule$ ,hich ha-e $ame chemical formula but
,ith different $tructure ,ith different $tructure
@+am'le : gluco$e and fructo$e @+am'le : gluco$e and fructo$e : : C C
D D
/ /
# #
O O
D D
3 an, 4 iso+ers iso+ers
@+am'le : @+am'le : G 1 gluco$e and 1 gluco$e and H H 1 gluco$e 1 gluco$e
"ith $i+ carbon atom$ numbered! "ith $i+ carbon atom$ numbered!
At Carbon , At Carbon ,
G gluco$e E ha$ O/ do,n gluco$e E ha$ O/ do,n
H gluco$e E ha$ O/ u' H gluco$e E ha$ O/ u'
1ISACC$ARI1ES 1ISACC$ARI1ES
?i$accharide$ are formed ,hen t,o mono$accharide 7oined together
Phy$ic characteri$tic Phy$ic characteri$tic
1 S,eet 1 S,eet
1 $oluble in ,ater! 1 $oluble in ,ater!
1 Can be cry$talli6ed 1 Can be cry$talli6ed
Chemi$try characteri$tic Chemi$try characteri$tic
1 1 Reducing Benedict te$t 3e+ce't $ucro$e5 Reducing Benedict te$t 3e+ce't $ucro$e5
A mono$accharide able 7oined together to form it by a A mono$accharide able 7oined together to form it by a conden$ation reaction! conden$ation reaction!
By hydroly$i$ reaction to form mono$accharide!
Ty'e$ of ?i$accharide Ty'e$ of ?i$accharide
Malto$e : Malt $ugar, an ingredient for bre,ing beer, reducing $ugar!
Sucro$e :Source $ugar1cane, in 'lant 3main form that i$ tran$'ortation in 'lant5, non1
reducing $ugar!
&acto$e :found in mil0 and, im'ortant energy $ource for young mammal$, can only be
dige$ted $lo,ly!
For+ation o" ,isa&ari,e For+ation o" ,isa&ari,e
The t,o mono$accharide 7oined together by a conden$ation reaction$ in ,hich ,ater i$
remo-ed
The bond formed bet,een t,o mono$accharide a$ a re$ult of conden$ation i$ called
%l!osi,i /on,
A %l!osi,i /on, can al$o be bro0en do,n to relea$e $e'arate monomer unit$! Thi$
i$ called &!,rol!sis becau$e water is nee,e, to $'lit u' the bigger molecule
Malto$e, malt $ugar Malto$e, malt $ugar : : G gluco$e 4 G gluco$e G gluco$e 4 G gluco$e
Sucro$e, table $ugar Sucro$e, table $ugar : : G G gluco$e 4 G fructo$e ! G fructo$e !
&acto$e, mil0 $ugar &acto$e, mil0 $ugar : : gluco$e 4 galacto$e gluco$e 4 galacto$e
;ormation of di$accharide : Malto$e ;ormation of di$accharide : Malto$e
lacto$e lacto$e
Mil0 $ugar, i$ found e+clu$i-ely in mil0 and i$ an im'ortant energy $ource for young Mil0 $ugar, i$ found e+clu$i-ely in mil0 and i$ an im'ortant energy $ource for young
mammal$ mammal$
It can only be dige$ted $lo,ly, $o gi-e$ a $lo, $teady relea$e of energy! It can only be dige$ted $lo,ly, $o gi-e$ a $lo, $teady relea$e of energy!
&acto$e B gluco$e 4 galacto$e &acto$e B gluco$e 4 galacto$e
;ormation of di$accharide : Sucro$e ;ormation of di$accharide : Sucro$e
Reducing $ugar Reducing $ugar
All mono$accharide$ and $ome di$accharide 3malto$e and lacto$e5 are ty'e of chemical All mono$accharide$ and $ome di$accharide 3malto$e and lacto$e5 are ty'e of chemical
reaction 0no,$ a$ reduction! reaction 0no,$ a$ reduction!
Sucro$e 3non reducing $ugar5 and 'oly$accharide can<t reducing Benedict te$t! Sucro$e 3non reducing $ugar5 and 'oly$accharide can<t reducing Benedict te$t!
Reducing $ugar : +altose
*on reducing $ugar : surose
POL5SACC$ARI1ES POL5SACC$ARI1ES
Are formed ,hen many hundred$ of mono$accharide$ conden$e 37oin5 to form chain$! Are formed ,hen many hundred$ of mono$accharide$ conden$e 37oin5 to form chain$!
The chain$ formed may be: The chain$ formed may be:
1 Iariable in length Iariable in length
1 Branched or unbranched 1 Branched or unbranched
1 ;olded E ideal for energy $torage 1 ;olded E ideal for energy $torage
1 Straight or coiled 1 Straight or coiled
Characteri$tic of 'oly$accharide$: Characteri$tic of 'oly$accharide$:
1 1 large, large,
1 not $,eet 1 not $,eet
1 In$oluble in ,ater 1 In$oluble in ,ater
Pol!sa&ari,es are 'olymer$ of hundred$ to thou$and$ of mono$accharide$ 7oined
by glyco$idic lin0age$!
;unction : i$ a$ an energy $torage macromolecule that i$ hydroly6ed a$ needed!
Other$ : $er-e a$ building material$ for the cell or ,hole organi$m!
STARC/ STARC/
Star& Star& i$ a $torage 'oly$accharide in 'lant$! i$ a $torage 'oly$accharide in 'lant$!
monomer$ are 7oined by 1( lin0age$ bet,een the monomer$ are 7oined by 1( lin0age$ bet,een the G G gluco$e, 0no,n a$ gluco$e, 0no,n a$ G1,( glyco$idic G1,( glyco$idic
bond bond ! !
unbranched form of $tarch unbranched form of $tarch : : amylo$e amylo$e : : form$ a heli+! form$ a heli+!
Branched form$ Branched form$ : : amylo'ectin! amylo'ectin!
A+!lose A+!lose
Made from G1gluco$e molecule$ Made from G1gluco$e molecule$
;orming unbranched helical chain of %99 unit$ in length! ;orming unbranched helical chain of %99 unit$ in length!
@ach G1gluco$e i$ 7oined by a glyco$idic bond bet,een neighbouring C and C( atom$! @ach G1gluco$e i$ 7oined by a glyco$idic bond bet,een neighbouring C and C( atom$!
A+!lo'etin A+!lo'etin
Made from G1gluco$e molecule$ Made from G1gluco$e molecule$
;orming branched chain$ of u' to )99 unit$ ;orming branched chain$ of u' to )99 unit$
Branche$ occur e-ery %9 unit$ and are formed bet,een neighbouring C and CD Branche$ occur e-ery %9 unit$ and are formed bet,een neighbouring C and CD
atom$ ,hich are then held together by glyco$idic bond! atom$ ,hich are then held together by glyco$idic bond!
amylo$e
amylo'ectin
6l!o%en 6l!o%en
Animal$ al$o $tore gluco$e in a 'oly$accharide called Animal$ al$o $tore gluco$e in a 'oly$accharide called %l!o%en %l!o%en! !
Clycogen i$ highly branched, li0e amylo'ectin! Clycogen i$ highly branched, li0e amylo'ectin!
;ound in li-er and mu$cle ti$$ue and made u' of $hort branched chain$ of G1gluco$e ;ound in li-er and mu$cle ti$$ue and made u' of $hort branched chain$ of G1gluco$e
unit$! unit$!
Cellulose Cellulose
Ma7or com'onent of the tough ,all of 'lant cell$! Ma7or com'onent of the tough ,all of 'lant cell$!
&ong chain$ of &ong chain$ of 4.%luose 4.%luose unit$ ,hich are unbranched unit$ ,hich are unbranched
but 'arallel $trand$ of cellulo$e are lin0ed by mean$ of hydrogen bond$, ma0ing the but 'arallel $trand$ of cellulo$e are lin0ed by mean$ of hydrogen bond$, ma0ing the
cell ,all a -ery $table $tructure! cell ,all a -ery $table $tructure!
The en6yme$ that dige$t $tarch cannot hydroly6e the beta lin0age$ in cellulo$e! The en6yme$ that dige$t $tarch cannot hydroly6e the beta lin0age$ in cellulo$e!
Cellulo$e in our food 'a$$e$ through the dige$ti-e tract and i$ eliminated in fece$ a$ Cellulo$e in our food 'a$$e$ through the dige$ti-e tract and i$ eliminated in fece$ a$
Jin$oluble fiberK! Jin$oluble fiberK!
A$ it tra-el$ through the dige$ti-e tract, it abrade$ the inte$tinal ,all$ and $timulate$ A$ it tra-el$ through the dige$ti-e tract, it abrade$ the inte$tinal ,all$ and $timulate$
the $ecretion of mucu$! the $ecretion of mucu$!
Some microbe$ can dige$t cellulo$e to it$ gluco$e monomer$ through the u$e of Some microbe$ can dige$t cellulo$e to it$ gluco$e monomer$ through the u$e of
cellula$e en6yme$! cellula$e en6yme$!
/erbi-ore$, li0e co,$ , ha-e $ymbiotic relation$hi'$ ,ith cellulolytic microbe$, allo,ing /erbi-ore$, li0e co,$ , ha-e $ymbiotic relation$hi'$ ,ith cellulolytic microbe$, allo,ing
them acce$$ to thi$ rich $ource of energy! them acce$$ to thi$ rich $ource of energy!
Co,$ do ha-e en6yme$ Co,$ do ha-e en6yme$ : : amyla$e$, ,hich can brea0 amyla$e$, ,hich can brea0 H H 1 ,( glico$idic bond$ in 1 ,( glico$idic bond$ in
$tarch but ,hich cannot recogni6e $tarch but ,hich cannot recogni6e H H 1 ,( glico$idic bond$ in cellulo$e, 1 ,( glico$idic bond$ in cellulo$e,
the bacteria in the rumen do 'roduce en6yme$ called cellulle$ ,hich can recogni6e the bacteria in the rumen do 'roduce en6yme$ called cellulle$ ,hich can recogni6e
and brea0 and brea0 H H 1 ,( glico$idic bond$ in cellulo$e 1 ,( glico$idic bond$ in cellulo$e
TOPIC 1 : MOLECULES OF LIFE
Retol, /!7
A+ran M, Sai,
Matriulation Colle%e o" Pa&an%
1.# LIPI1S
Ceneral term for any ,ater1in$oluble organic molecule$ that can be e+tracted from
cell$ by ether$, ben6ene, or other non'olar $ol-ent$!
They contain carbon, hydrogen and o+ygen, ,ith far more hydrogen and carbon
com'ared ,ith o+ygen than in carbohydrate$A
They are in$oluble in ,ater !
% ma7or cla$$e$ of li'id$
! triglyceri$e$ : e!g! ;at L oil
#! 'ho$'holi'id$ : e!g! &ecithin
%! $teroid$ : e!g! Chole$terol L Te$to$terone
Im'ortance of li'id$
@nergy $torage
Com'onent of cell membrane
In$ulation : blubber
@mul$ifier$
Im'ortant carrier$ or 'recur$or$ of im'ortant fla-or and odor com'ound$!
Tran$'ort$ fat1$oluble -itamin$
Immune $y$tem
Contribute$ to obe$ity, coronary heart di$ea$e and other health 'roblem$!
TR>C&>C@RI?@
Com'o$ed of % fatty acid molecule$ attached to a glycerol bac0bone

Triglyceride$ ,ith releti-ely $hort fatty acid chain$, or ,ith un$aturated fatty acid$, tend
to be li.uid at normal tem'eraturated and called oil$!
Triglyceride$ ,ith longer fatty acid chain$, or ,ith $aturated fatty acid, are more li0ely
to be $olid and are called fat$!
Triglyceride$, li0e all li'id$, are in$oluble in ,ater! Thi$ i$ becau$e they ha-e no di'ole$
and no charge$ ,hich can attract ,ater molecule$!
Are e$'ecially u$eful a$ energy $tore$, becau$e they contain much energy 'er gram
than either carbohydrate$ or 'rotein$!
;ormation -ia conden$ation
brea0do,n by hydroly$i$
;ATT> ACI?S
&ong linear hydrocarbon chain$
One end 1 contain$ a carbo+ylic acid grou'
The other end i$ the methyl, MnM or omega end!
Cla$$ification of fat$ ba$ed on fatty acid$
! Saturated fat : $aturated fatty acid : eg! Stearic acid
#! Un$aturated fat : un$aturated fatty acid : eg! oleic acid
Cla$$ification of e$$ential
@$$ential fatty acid$
1 Body can<t 'roduce o,n fatty acid$, $o it<$ needed from food!
*on1e$$ential fatty acid$!
Body can $ynthe$i$e fatty acid$ it$elf
P/OSP/O&IPI?S
@+am'le : &ecithin 3in cell membrane $tructure5!
Im'ortance of lecithin in cell membrane $tructure:1
Polari6ation lead$ to $olubility in ,ater! It act a$ a 'ermeability barrier, $o that
e+change$ acro$$ thi$ membrane are -ery limited and -ery $lo,!
Permeable to ,ater molecule$, but not to ion$ $uch a$ *a
4
, F
4
, and Cl
1
!
ST@ROI?S
@+am'le$ : Chole$terol L Te$to$terone!
Structure of Steroid$!
PROTEI0
At the end of the le$$on, $tudent $hould be able to:
?e$cribe the ba$ic $tructure and cla$$e$ of amino acid$
@+'lain ho, amino acid$ are grou'ed
?e$cribe the formation and brea0do,n of di'e'tide
@+'lain $tructure le-el$ of 'rotein$ and the ty'e$ of bond$ in-ol-ed
@+'lain the effect of '/ and tem'erature on the $tructure of 'rotein
Cla$$ify of 'rotein$ according to their $tructure
Protein
Protein are 'olymer$ ,ho$e molecule$ are made from many amino acid molecule$
lin0ed together!
Protein con$i$t$ of carbon, hydrogen, o+ygen and nitrogen!
;unction of 'rotein:
1 @n6ymatic cataly$i$ !
1 Tran$'ort of re$'iratory ga$e$ and $torage!
1 Structure and $u''ort
1 Contact$ or co1ordination 3hormone$5
1 Immunity!
1 Cro,th and de-elo'ment E membrane 'rotein$!
1 /eredity
Protein molecule
@ach different 'rotein$ molecule i$ made under the direction of it$ o,n gene and
'erform$ it$ 'reci$e function!
The $ha'e of it i$ determined by it$ amino acid$ $e.uence!
Amino acid$ are the building bloc0$ from ,hich 'rotein are made!
There are about #9 commonly occuring amino acid$ in 'rotein!
All ha-e the $ame ba$ic $tructure but differ in their R@SI?UA& C/AI* 3 R 5!
Amino Acid Structure
An amino acid i$ a molecule containing an amino grou' 31*/
#
5, a carbo+yl grou' 31
COO/5, and a hydrogen atom!
Amino grou' 31*/
#
5 ha$ characteri$tic$ $uch a$ ba$ic!
Carbo+yl grou' 31COO/5 ha$ characteri$tic$ $uch a$ acidic!
@ach amino acid ha$ uni.ue chemical 'ro'ertie$ determine by the nature of the $ide
grou' 3indicated by R5!
;or e+am'le, ,hen the $ide grou' i$ EC/
#
O/, the amino acid 3$erine5 i$ 'olar, but
,hen the $ide grou' i$ EC/
%
, amino acid 3alanine5 i$ non'olar!
Ty'e of amino acid, Ba$e on $ide chain grou' N
1 Polar : eg! Serine 3Ser5
1 *on 'olar : eg! Clycine 3Cly5
1 Acidic : eg! A$'artic acid 3A$'5
1 Ba$ic : eg! &y$ine 3&y$5!

;ormation of Poly'e'tide$
T,o amino acid$ can be 7oined by a conden$ation reaction to form a di'e'tide!
If any amino acid$ are 7oined together by 'e'tide bond$ then a 'oly'e'tide i$ formed!
A 'oly'e'tide u$ually contain$ hundred$ of amino acid$!
The re'eated $e.uence 31*1C1C1*15 i$ the 'oly'e'tide bac0bone!
amino acid$ are $tructure of 'rotein
The t,enty commonly occurring amino acid$ can be arranged in an enormou$ -ariety
of different ,ay$ in gi-ing ri$e to many different 'rotein$
A 'lant can $ynthe$i$ all amino acid$ a$ needed from $im'le com'onent!
But an animal can<t $ynthe$i$ a'art of amino acid$
Ba$e on e$$ential, amino acid$ di-ide # categorie$
i5 @$$ential amino acid E eg! Methionine, ly$ine and Ialine
ii5 *on1e$$ential amino acid E eg! Clycine, alanine and Cy$teine!
Structure of 'rotein$
A ty'ical 'rotein con$i$t$ of one or more 'oly'e'tide chain$ ,hich may be folded,
branched and cro$$1lin0ed at inter-al$!
@ach 'rotein$ ha$ a $'ecific three1dimen$ional $ha'e!
In de$cribing the $tructure of a 'rotein, it i$ u$ual to refer to four $e'arate le-el$ of
organi6ation!
Primary 3
9
5, $econdary 3#
9
5, tertiary 3%
9
5 and .uaternary 3(
9
5 le-el$ of 'rotein!
Primary $tructure
Thi$ di$cribe the $e.uence of amino acid$ in the 'rotein and u$ually determine$ it$
e-entual $ha'e and biological function!
Secondary $tructure
Once a linear chain of amino acid$ i$ formed it $'ontaneou$ly fold$ to form G heli+ or H
'leated $heet!
/ydrogen bond$ hold$ the $econdary $tructure together!
Tertiary $tructure
Once they ha-e been folded by hydrogen bond$, 'oly'e'tide$ may then fold into a
globular $ha'e ,hich i$ maintained by
1 hydrogen bond$,
1 ionic bond$
1 di$ul'hide bridge
@+am'le myoglobin!
/ydrogen bond E bond bet,een 'olar $ide chain$
Ionic bond E bond bet,een 'o$iti-ely and negati-ely charged $ide chain$
di$ul'hide bridge 3co-alent bond$ bet,een $ul'hur atom$ in the re$idual chain$ of the
amino acid$!5
/ydro'hobic interaction$ L -an der "aal$ interaction$ E *on'olar R grou' ,ith
another non'olar R grou'
Ouaternary $tructure
Con$i$t$ of more than one 'oly'e'tide chain$ to form a $ingle functional molecule
/eld together by hydro'hobic interaction$, hydrogen bond$, ionic bond$ and di$ulfide
bridge$
A$$ociated ,ith non1'rotein grou'$ into a large com'le+ 'rotein molecule
/uman haemoglobin i$ an e+am'le!
It con$i$t$ of four chain$ 3t,o G1'oly'e'tide chain$ and t,o H1'oly'e'tide chain$5
,ra''ed around an iron hem grou'!
@ffect of '/ and tem'erature on $tructure of 'rotein
Structure of 'rotein maintain by hydrogen bond 3 # , % and (5A ionic bond, hydro'hobic
interaction, di$ulfide bridge and -an de ,aal$ interaction 3 %, (5
Brea0age the bond cau$e$ lo$$ of $'ecific three1dimen$ional $ha'e of a 'rotein
molecule
They change may be tem'orary or 'ermanent
But amino acid $e.uence remain$ unaffected
Change $ha'e of 'rotein E denaturation
?enaturation occur$ under e+treme condition$ $uch a$ e+treme '/ and tem'erature!
Molecule unfold$ and can no longer 'erform it$ normal biological function
If the tem'erature or '/ e+ceed$ a 'rotein<$ range of tolerance, it$ 'oly'e'tide
chain$ ,ill un,ind or change $ha'e, cau$ing to lo$e it$ conformation and hence it$
ability to function
@+am'le: Protein$ are ea$ily damaged by heat 3tem'erature$ greater than (9
9
C5 due
to brea0age of their cro$$ lin0age$
Thi$ cau$e the 'rotein molecule$ to o'en u', $traighten the fold$ and a$$ume a
random configuration
;or $ome 'rotein$, denaturation might be re$er-ed ,hen normal condition$ are
re$tored
Cla$$ifation ba$e on $tructure
?i-ided by % cla$$ification ba$e on $tructure!
1 Con7ugated 'rotein
1 Clobular 'rotein
1 ;ibrou$ 'rotein
Con7ugated Protein
'rotein 7oined ,ith non 'rotein com'onent8 'ro$thetic grou'
Protein $tructure merge ,ith ,ith non 'rotein grou' 3'ro$thetic grou'5
@g! /aemoglobin contain$ the 'ro$thetic grou' containing iron, ,hich i$ the haem! It i$
,ith in the haem grou' that carrie$ the o+ygen molecule through the binding of the
o+ygen molecule to the iron ion 3;e
#4
5 found in the haem grou'
Clobular Protein
Mo$tly, that 'rotein related in tertiary and .uaternary $tructure!
U$ually ,ater $oluble 3can to form colloid5
&ong 'oly'e'tide ,ith heli+ to form globular or $'herical
e+am'le: globulin 3blood $erum5, en6yme$, antibody, hormone
;ibrou$ Protein
Mo$tly, that 'rotein related in $econdary $tructure!
In$oluble in ,ater and -ery $trong becau$e it$ ma0e from long 'oly'e'tide
e+am'le: collagen, myo$in, fibrin and 0eratin
?ifference$ bet,een fibrou$ 'rotein and globular 'rotein$
Pro'ertie$ of 'rotein
Am'hoteric
Buffering ca'acity
Colloidal 'ro'ertie$
?enaturation
*ote :
Pro'ertie$ of Protein, 7u$t for e+tra 0no,ledge
Pro'ertie$ of 'rotein
! Am'hoteric
In a.ueou$ a$ neutral 3'/ P5, amino acid $uch a$ di'ole, it$ called 6,itterion$
Am'hoteric becau$e ha-e characteri$tic both acidic and ba$ic!
In a.ueou$ acidic 3Q '/ P5, 'rotein recei-e /
4
and ma0e it$ 'o$iti-e charge!
In a.ueou$ al0aline 32'/ P5, donate /
4
and ma0e it$ negati-e charge!
Charge at 6,itterion$ de'end on '/
'/ at amino acid a$ neutral li0e electric it$ call i$oelectric
All amino acid$ ha-e o,n characteri$tic a$ i$oelectric 'oint 3'I5!
#! Buffering ca'acity
Am'hoteric characteri$tic of amino acid$, it$ ma0e $uch a$ buffer
A buffer $olution i$ one ,hich re$i$t the tendency to alter it$ '/ e-en ,hen $mall
amount$ of acid or al0ali are added to!
That mean a buffer $olution can<t change $'ontaneou$ly, ,hile added '/ increa$e
3ba$ic5 ! Amino acid$ ,ill donate hydrogen ionic!
"hile '/ reduce 3acidic5, amino acid$ ,ill recei-e hydrogen ionic!
%! Colloidal 'ro'ertie$
(! ?enaturation
The $tructure of a 'rotein can be change if the bond$ ,hich hold it in $ha'e are
bro0en! Thi$ 'roce$$ i$ called ?enaturation!
/igh tem'erature$ brea0 hydrogen bond and -an der "aal$ force$! In a globular
'rotein a long chain in$tead of a curled1u' ball! The molecule$ ,ill no longer be $oluble
in ,ater!
@+treme$ of '/ brea0 ionic bond, becau$e they alter the charge$ on R grou'$!
Reducing agent$ brea0 di$ul'hide bond! Thi$ i$ made u$e of ,hen 'erming hair!
Feratin, from ,hich hair i$ made, contain$ di$ul'hide bond that hold the $ha'e in
$ha'e!
0UCLEIC ACI1
To'ic di$tingui$h
At the end of the le$$on, $tudent$ $hould be able to:
?e$cribe the $tructure of nucleotide a$ the ba$ic com'o$ition of nucleic acid 3?*A and
R*A5
?e$cribe the $tructure of ?*A ba$ed on the "at$on and Cric0 Model!
State the ty'e and function of R*A
State the difference$ of ?*A and R*A

*ucleic acid$
The amino acid $e.uence of a 'oly'e'tide i$ 'rogrammed by a gene!
A gene con$i$t$ of region$ of ?*A, a 'olymer of nucleic acid$!
?*A 3and their gene$5 i$ 'a$$ed by the mechani$m$ of inheritance!

Structure of nucleotide
*ucleic acid$ are 'olymer$ of monomer$ called nucleotide$!
@ach nucleotide con$i$t$ of three $maller molecule$! The$e are :
! A 'ho$'hate grou'
#! A 'ento$e $ugar
%! A nitrogenou$ ba$e
Pho$'hate grou'
Pento$e $ugar
*itrogenou$ ba$e
% com'onent$ are combined by CO01E0SATIO0 reaction!
% com'onent$ are brea0do,n by $51ROL5SIS reaction!
10A
?ouble $tranded 'olymer of nucleotide$
Contain$ ( ba$e$ 3not include uracil 3U5 5:
i!Adenine 3A5
ii!Cuanine 3C5
iii!Cyto$ine 3C5
i-!Thymine 3T5
&ong and thin $trand
Amount bet,een A and T and C and C u$ually e.ual to each other becau$e A al,ay$
'airing ,ith T and C ,ith C
/eli+ $ha'e i$ maintained by />?ROC@* BO*?S
Rame$ "at$on and ;ranci$ Cric0 'o$tulated double heli+ of # nucleotide$ $trand$
*ucleotide $trand$ being lin0ed together by 'air$ of nitrogenou$ ba$e$ ,hich are
7oined by hydrogen bond$
Purine$ A double ring $tructure$ form longer lin0$ if 'aired together than 'yrimidide
Only by 'airing 'urine ,ith 'yrimidine E con$i$tent $e'aration of % ring$< ,idth can
be achie-ed
?eo+yribo$e and 'ho$'hate unit$ form the u'right$ ,hile nitrogenou$ ba$e 'airing$
form the rung$
# chain$ that form the u'right$ run in o''o$ite direction 3anti'arallel5
R*A
Single $tranded 'olymer of nucleotide$
Pento$e $ugar E ribo$e
Organic ba$e$ E Cuanine, Cyto$ine, Adenine and Uracil 3re'lacing thymine5
% ty'e$ of R*A :
i!Me$$enger R*A 3mR*A5
ii!Tran$fer R*A 3tR*A5
iii!Ribo$omal R*A 3rR*A5
rR*A
&arge,com'le+ molecule
Made u' of double and $ingle heli+
Manufactured by ?*A of the nucleu$
;ound in ribo$ome
Com'ri$e$ of more than half the ma$$ of the total R*A of the cell
The Ba$e $e.uence i$ $imilar in all organi$m$
tR*A
Small molecule, com'ri$ing $ingle $trand
Manufactured by nuclear ?*A
Made u' 9 1) S of cell<$ R*A
All ty'e are fundamentally $imilar
;orm clo-er1leaf $ha'e, one end of the chain ending ,ith C1C1A $e.uence
"hich amino acid attache$ it$elf
T #9 ty'e$ of tR*A, carrying different amino acid
At an intermediate 'oint along the chain i$ an im'ortant $e.uence of % ba$e$ E
anticodon
mR*A
&ong $tranded molecule, u' to thou$and$ of nucleotide$ form into heli+
Manufactured in nucleu$
Mirror co'y of a 'art of a $trand of ?*A
There i$ hence an immen$e -ariety of ty'e$
@nter the cyto'la$m E a$$ociate ,ith ribo$ome$ and act$ a$ tem'late for 'rotein
$ynthe$i$
Made u' le$$ than )S of total cellular R*A
@a$ily and .uic0ly bro0en do,n, $ometime$ e+i$ting for only a matter of minute$!
@dited on Mei, % #9
Retold by,
Amran Md Said
Matriculation College of Pahang
The @nd 1

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