Professional Documents
Culture Documents
Biomolecules
Biomolecules
Biomolecules
t; !\rj
·Q1Jillct]GBI0 Ji1
After stuctYtn.
ab to g this Untt, you wtll be i111111 tt'fMMit, 1
0 .r
3 Triose Ketotriose
4 Tetrose·. dotetrose Ketotetrose
5 Pentose Aldopentose Ketopentose
6
('
Hexose Aldohexose Ketohexose ·
7 Heptc:>se. Aldoheptose Ketoheptose
. I
. ,.....
. - - -~
14.1.2.1 Glucose occurs freely in riatur ··w
sand ho
Preparation of
Glucose ;..i,::;;~~~r~~~ If sucrose is boiled with dilute HCl or
, glucpse and fructose are obtained in
I
I I
stt11ctir of Gluco _:::;::~~~:
~ . Glucose:==1=........
b4 lgf Biomolecules
. CHO COOH
I, I . ··cooH
OXidatto~ I ,,
(CHOH)4 (C'.HOH) f.xidatlon
I . ,4 (CHOH)
CH20H
I . ' I 4
COOH , CH20H
Saccharic Glucontc
acid acld
:;;,;_;:-ct spatial arrangement of different-OH grou ·
s·c he er ~tudying many other properties. Its corilis was given
co,,.ri.,~ represented as I. So glucontc acid is representeration 1s
sacchartc acid as·m. •. · as Dand
/~Li~~
.. c11$\ · ·- CHO
.4 ~;de .
HOt o:
(-) - Glyceraldehyde
. Chemistry -~
' '' ·.. \ ~, ~1(\ ~ , , ,_.,
M~l-h¼po i~ '.f- ,,pm~_.
the co . I
(Ju't\~-> r~ 7o<J
etrtc carb<>n
atom a · tlon of mpnosaccharldes, It ts the lc,WeSt ~ s e -OJ-I on
the :!Jsshown,below) which ls compared. As ln (+) gl~18 co~parable
- t o (+)10 t asymm_etrt~ carbon ts on the rtght stde whic tton. Qtber
a glyceraldehyde, so (+) glucose ls assigned D-conftgura d for this
symmetric carbon atoms of glucose are not constdere tten
~ n. Also, f g!ucose and gtycerald~ ~ ts ,_.. "
a way lhat ost oxidised carbo (hi1fitscase - CHO ls at e to .
CHO ·
~;
I
I
H i OH
H
__ --~~-,
OH I
I
: _______
CH2OH
___ ,:
=-
._
s
- H-~~ H- f . HO- ~ . .
H I· ~-OH I .li 2 j ff · ~H I
HO 3 H O HO 3 ~ . ,HO l H. 0
H4 OH
H4 OH
H _ _ __, .H 5
5 --
6 6
CH2 OH •CH
' 2 OH
H OH
H OH
a - D - (+) - Glucopyrariose · /J:_ D - (+) - Glucopyr~0,
1·
2117I
.tto -9-ettptt
. HOw
H
·H
OH
0 4 H0~4
H
H
OH ·
0
H 5 H 5
6 6 .
CH2 0H CH2 0H
a - D - (-) - Fructofuranose P- D - H - Fructofuranose
: t'~l
re__d~ f'W(l(2~
ct
'
rnon~~~ <lr,d
1 HOH2C~
H
- 0
H
4
OH · OH
CH20 H .
.
HOH2C
-~ H
H 4
OH .
CH,OH
O . OH
examp e,
accharides is sucro on
· · gtves equimolar mixture ofD-(+)-glucose and D-(-) fructose.
c 12 H 22 0 11 + H20
Sucrose
c H O +· Cs H12 0 6 s 12 s
t>(i d; o D-(+)-Glucose • D-(-)-Fructose
\ "\l()·S°" o<= Q.~ c( -:_q)_. 4 0
l j----:---,
• • • •
-- H O I
HO
----=-~
3
L-------
Qfl Glycosidic
2 I · I
- ;-;. H
- linkage OH H
hydrolysis gives
ctose. Since the
~i;,;.;;,.,,;;;.;.;;.;.~----:---:"" of
l
0
3 3
H OH H OH
. {I) (II)
a- D - Glucose a- D - Glucose
Maltose
,4~ Biom olecules
~ lose: It to more commonly known ~;;,i.,;.,1.7"
Ince thts
milk. It ls comp .....~-...;;.;;.~ a.net
f ffi~ ~ ---;~~~- ge-rs between Cl 4 or
y e group may be produce at C-1 of gI~~
un'It.bence It ts also a reducing sUS,!ll'•
e e
CH1 0H . CHiOH
H
0
H OH -H OH
/J- D - Oalactose {J - D - Glucose
(i4.1.4 -Lacto1e ·
i_!o1Jaaocharlde1 , _ Polys~cchartdes contaJn-a~large number of monosacc ~~WHS:-fehi
together by glycosidic linkages_. Th~e~s;;e~ ar~e=th~e~~~:::'!~~
!?ncountered carbohydrates in nature. They mainl
stor~ r strtffifuiirmatenals .
.-;;:---;----iv--
• Ptnftxt.
ft fl) to
--,._....:._~
---"-- -> ~l,.tt
'" lrrtu"I
.:~=
Starch: S
is a polymer
..--- -~..;;;.:.;;;~~"!"::":::-::-t::i:~'Tfr.~::..!! ts
lea. 1!
t
s
,n -~ n( _.. . ~d.UUJ;'\
. ', uuu QJY\
· ~ ~ J ) Jlllrr-M . ·
()
H OH_, -r-- H H OH
a-Link a-Link
Ainylo1e
H i
a•Unk a-Unk
/ Amylopeotlll
J,ff[ Cellulose: Cellulose occurs exclusivel lants and it is the most
abundant organic substance plan g . I~ inant
qo~s~ituen o ce o pan . ose - ~chain,
HOHaC I
O
H
?:-0~ OH
. HOHaC -~ -
~ ~-- ·_ _:::..
OH - - -~ ,8-links
- - OH ·: -
1
. . .Cellul~o•;;;;•~ ~ ~ ,
polysaccharlde composed only
joined by glycosidic link:aicg~e~ ~ ~ ~ ~ ~ ~ ~.
· _...,e4 of the next_glucose unit.
y((ii) Glycogen: The-carboh .
It is also known a animal s
amylopectln and is ra
14.1.5 Carboh
Importance of e
Carbohydratei as an ~ =~~ ;:::;irnj~=f::~ ;:!:~t-=:'::=:":r
medic ch in
plants'an ycogen in animals. Cell wall dfbacterla'aQd plants is
made up of cellulose. We build furniture, etc. fr"om.oellule~ in the form
l 9 Biomolecul~s
',' ,, -•~1/lf J
or wood and clothe ourselves With cellulose Jn the fo .
Tfiey provide raw materials for manYfmportruit indu ~ of cottol}Jlhre
8
pap~r, lac uers apd breweries. es Uke textiles·
. rudop'eltyo!;s~ vt -ribo -deoxy-n rib '
' 14.5.1, la"SS""XfTI are p esent nucleic actds. . hy- 0 (Sectton
tn biosystem in combination With many proteins and li es are foUnd
P1ds. ,
lntext Qu,estions
liA,.; Glucose or sucrose are soluble in water but cyclohexan
benzene (simple six membered ring compounds) are insolub~ :
/ water. Explain.
~ ~-1 /What are the expected products of hydrolysis of lactose?
J"3 How do you explain the absence of aldehyde group in the
pentaacetate of D-gluc~se?
14.2 11roteins
Proteins are the livin~~ Ill.
•111' ---:) \.ll.u tde r) Chief sources of pro
etc. They occur in every p o
ean'tttt'if~ ear.,-
e o Y an omi the fundam~
basis of strudure and functions of life. They ~e also required for
gro~ and maintenanc_e o . The word tett::~ •
Greek word, '1,roteios" whi ·
All proteins are olymers o ~~~-"""""~--~.;.;~~~
14.2.1 Amino Amino acids contain amino (-NH2) and carboxyl (-COOH) functtona)
Acids groups. Depending upon the relative position of amino group With
respect to carboxyl group, the amino acids can_ be R- CH_
classified as a, ~. y, 8 and so on. Orur a-ammo I C00H
acids are obffi!11ed o~ l~s~ of p roterrµ, . They NH
may ·contain.o1rier ruhtfional groups also. 2 acid
a ~ammo
All a-amino acids have trivial names, which (R = side chain)
usually r~ e property of that compou
its s o u r c ~ i named since it ha s~ ee ste (in Greek glykos
means sweet) an tyfosm was s o e in Greek, tyros
means cheese.) acids are enei-all re er
,_symbol, sometimes one letter symbo is so used. Structures of some
commonly occurring .amino acids along with their 3-lctter and I -letter
· symbols are given in Table 14.2.
. . .JOOH
· ~ • 14.2: N&~;{AmfDo Adds H,NT H
~-J ~ - . . R
. .
'ij Gly G
- J ~_!:::la Ala A
Jl:IaCJ2Cl:I- ·:, Val V
(HaCJ2CH-CHr .. ,Leu ·L
. Ch, mistry 4;',
-
Proline has no nh2 group
I C
lie
®
II
H2N-C-CH 2-CH2- pin
.0
ragine
nine\/'
II
· H2N-C-CH2- Asn 0T
hl3C-CHOH- Thr
HO-CH 2- ,, Ser s
'
nif · HS-CH 2- Cys C
nine:,,- H3C-S-CHrCH2- Met M
lalanine• .
iv
· CsHs-CH2-
(p)HO-CJ¾-CH2-
Phe
Tyr ffi LJ
ro
-CH2
' Trp
H
His H
Pro p
1-4.2.2
Amino acids are classified as acidic, basic or neutral depen(iing upon
Classification of the relative number of amino and carboxyl groups in their molecule.
Amino Acids Equal number of amino and carboxyl groups makes it neutral; more
number of amino than carboxyl groups makes it basic and more
carboxyl gro~ps as compared to amino groups makes it acidic.'. The
amino acids, which can be synthesised in the body, are known,as non-
essential amino acids. On the other hand, those which __..
' ,.._...;:.:;.:;~~= cannot .be
..,._,...,,,_.,_.,...,.
synthesised in the bod and must be obtained ~ ugh diet; art:. known
en 1 a:,mo acid§ (marked with as ens m a e 4 . ~ .
Biomolecules
Amino acids are us ua ll co ourles lids. 1bese ,
water-soluble, high J}~ ng_s~lds. and be ave e s s rather ·thate
simple amines or carooxylfcacfcfs. This behaviour ls due fo the Presena.ti
of both acidic (carboxyl group) and baste (arn~e
0 o group) groups In the same molecule. In aqueo 0
II
R-CH- C- 0 - H II _ solution, the carboxyl group can lose a Prat I.ts
I R- CH - C- 0 and amino group can accept £-offiff;11:1. iving rto11
:NH:2 +~ 8 3 to a dlpolar ion known witter to . Thts ~:
(Zwttter'ton) neutral but contains 1 9oth pos negau,.,
charges. , e
In zwttter ionic form, amino acids show. amE_hotertc beh_!vtour as
they r oth with acids an~ ~s. ·
e all other naturally occurring a.-amJ.no actds ar
e, si~ceffi'eii:' e: ~ is asymmelrtc. Tiie~ ~
...~ ~ ~ ~ an~d'. , , forms. ost natur occurrtn 8e·
14.2.3 Structure You have already read that proteins are the polymers of ~-amino acids
of Proteinsand they are connected to each other by peptide bond or Peptide
linkage. C_hemically, , peJ;?tide linka_ge is an amide formed beS!:_een .
-COOH group and-NH2 group. The rea~tion between two molecules of -
- - • sfuillar or different amino acids, proceeds through
_~oj
H2N- CH2- COOH + H2N -yH - COOH the combination ~f the amino gro1.;1p of one molecuie
CH3 with the carboxyl group of the other. This results In
the eliminati9n of a water molecule and formation of
H2N - CH2-'-ICO - N~ -CH - COOH . .a pepW@ bofiif»-Cb=-Ntf-. ine°product of the reaction
j . I . is called a dipeptide because it is made-up of two
Peptide linkage_./ CH3 · amino ·acids. For example, when qarboxyl group of
· · glycine combines with the amfuo group of alanine
Glycylalantne (Gly-Ala) we get a dipeptide, v~l.~Y~ ~e. .
tU'b> ' If a third amino acid combines to a dipeptide, the product is-called a
!)t-.110 ~ "
,
1;~ t . . tripeptide. A trlpeptide contains three amtno·acids linked by two peptide
rn~ linkages. Similarly when four, five or six amino acids are linked, the respecttve
(!1 re'.l . , products are known as tetrapeptide, pentapepti tide
@ g'u.,.Qt- -k i\ . respectively. When the number of such amino ac s is more than t . '
i., c:lfOp theproductsarecalleg_~ tides.Apo- tidewt drea
OlMl'r\t Ji:P + l "'~ g ci,g r~ i~U£S~hf-vfii&iio~yprmass erth O,
· at,- ProteJ c1°'...J ro .11owever, llie filstinction betwee_n eoln,epti e , . pro e s
Ollb~ ~..JJ,.j_ r , -~- . n sh~..Polypeptldes wlth fewer amino adds are likely to be carrea~
. b~vt LCl'IJO . . p~ r e y ordinarU ~e a well deftnea conformation of a protein such
® M 1Ui'~r- ':, nc \ a lnsu which con s5 o acids. · ..
ot-f"_4~ol.l&l uw,'r
:.:-fbs:ir'nt~' .
o eins can be
molecular shape. ·
sstfied into two types on the basis of their
. , "-..
Q- Wtr-.'j ~ brous protetns , ·
J""l'. When the polyp . eptide. chains run parallel and are held together by
I> H' ' hl droge!1 an1 ~ sulphide bon,ds, then fibre- like structure ts formed. Such
I· ~ntelr\iY~ proteliis are ~enef ally inso~ water. Some common examples are
HNO~ (present in 1i.atr, w.2._~ !!1
an~yosin (present muscles}, etc.
~lobular proteins ..,
This structure results when the chains of po tides coll a~ - ~
to._g t as~ e shape. These a~ isua~ solu~l ~~ater ,!1~
herical
umln -e the coinmon exampfes o l!W-UW1ur1 protein ,..____~
re and shape-of proteins
- · can be studied at four dn i erent
levels, i.e., primary, secondary, tertiary and quaternary, each level
being more com&x than the previous one.
~ t{'Prt.mary structure of protetns: Proteins may have
one or more polypeptide chains. Each polypeptide in a
protein has amino acids linke.£"""1A~~-each other in a
'specific sequence and it is _ se uenc__Qf ~ o acids
C ...!2!t i~ sal<l to be the)@rn~ ~ .. e ofJ:hat prote~ ...
. Any change in this 'pninary structure I.e., the sequence
of ~ o acids creates a ~tfferent protein.
J}Jf' Secondary structure of protetns: The .secondary
· structure of protein refers to the shape in which a !ol_!S
H : · pol e tide chain can exist. They are found to exist in
· C J wo,_ · e ent types of structures vi~ nd
C ~-pleate beet structure. These structures arise· due
·f ~ o---W:e regular folding of the backbone of the polypeptide
! . 0
H chain due ~o hydrogen bonding between -~- and
-NH- groups of the peptide bond.
J
a-Helix is one of the
a ol e ec
'. /
y twisting into rt t _ (helix) wi e
\ Ji( 14.1: a-Helix '
-NH_ group o eac amino acid residue hydrogen on e to the
[.\ structure of proteins ,......c=o of an adjacent .. tum of the helix as shown in Fig.14.1.
.
I!!];!,1:;tct~ .~ are stretched opt
to nearly maximum extension and then laid side by side
N" W ;filch are nelcI together by interffiolef ular h drogen .
R(~[ RqH RCH b~ds. 4riie sfuicfure resemb es the pleated olas of
.. c.-.6 c ... 'c.,. dra~ and therefore is known as ~-pleated sheet.
O O
--H\( ....H,N,' ',H.. ¾~R .... ...)JK[rerttary structure ·o f proteins: The tertiary·
HpR HpR , structure of proteins represents overall folding of the
o•~N~ .... o"'9 . .H...... O"'~wH...- polypeptide chains i.e., f\u:!perJolding of the ~ec_2ndl;!Y
RCH · RC~
8 RCH ~ re. It gives rise to ~jor molecular shapes
'c 'C , viz. fibrous and· ar. · The main 'forces wh1ch
',H ... N •o...... H... •o... . .H.. lc"'O
N stab1llsi•,nr ~ ncl--3° structures of proteins are
. c
HpR
c. HCR ~CR
C
h~dro~~n bon , 1 e inkages, Vax;} dei:, W~al§.
and eib:!ostatlc force§! of attraction. · .,.,
/ - -. JJH('Quatern7:'ry structure of prot: ins: Some of the
fl· 14.2: /3-Pleated-sheetstructureof proteins are composed of two or more polypeptide
protefns chains referred, to as sub-;~.mits. The spatial.
ar@ngement of these subunits with rewct t~
ot!!~r Is Iaiown as quaternarystnictti're. - . - .....
·-~JO - - I
14&,31 Biomolecules
,., f i zt I! turf 197!.;
"
; I l j
· A ct1agrarnmatlcrepresentation of all these fb
gtven 1n Figure .14.3 where each coloured ballur 8~ctures ts
amJno acid. :" represents an
, ,
~•<:>
><::>·
"I
.I -. l •·,
~.
Jertfo/!J
J
' (a)
"
Prirnafy,.---_,_____. (b) Secondary- - --(cTTertlary
-
(d) Quatemaiy
and Jp.Wte1"[UUY -
structure I Structure structure structure
structure~ 9f ,
·• c'.i/ ' '· ~ ·• ·l \r • Rgroups
-~ to§§·
.
.·. .'
•H-- Oo .• Haeme group ·'
14.2.4 . .
;,
Denaturation of
is called~~~~5tei~m;-"a
Proteins
it ected to ~;al~~ge1 g~
in temperat1.1,re or -chemical change like change in pH, the ydrogen
~onds are distutbed ... Due to this, globules unfold and helix get uncoiled
and protein loses its biological activity. This is· called denaturation of ·
CheII1,istry t::'.!J' r
but
g ts
g of
~ Which
milk - is caused due to the formation of lactic act d bY e etm
Present in milk. ·
lntext uestions
14.4 The melting 0 in
higher th l:i
ts and solubtllty in water of amino acids are generally
an at of the corresponding halo acids. Explain.
14.5 Where does th
e water present in the egg go after boiling the egg?
/Lf~---------
fu mes Lili 1
e s possible due to the coordination of various chemical reactions in
livtng organtsms. An example is the digestion of food, absorption of
,d
(&QJJ.ls:frl appropriate molecules and ultimately production of energy• This process
' t·e..,rubi'n . {lVolves a sequence•of reactions and all these reactions occur in the
J, _ L _, c body under very coridftions, 'This occurs with the hel_P-
01 uw rue.. aafysts Calle enzymes. Almost all the e es ar lob~ a
• _ Ii •. protems Enzymes are very spec c or a p c ar reac on
'' Mb~ · substf~tt-,JI,hey are generally n~ed after the compound or
- - J.-. cl.ass of compounds upon which they work. For example, the enzyme
(J.RjfCtRf?j -~ . that catalyses hydrolysis of maltose into glucose is name4 as maltase.
~ S l'tt,ci(? . . C12H22<?u . . Maltase > 2 CaH120a
Maltose · G hicose
. Sometimes enzymes are also named after the reaction, where they
are us~q.. For·example, the enzymes which catalyse the oxidation of
one sub&trate with simultaneous reduction of anothe:i; substrate are
named as oxidoreduct,se enzymes. The ending of tl;ie name of an
enzyme
,, ·
is -ase:
14,3.1 Mec~anism
·or Enzyme Enzymes are needed only in small quantities for the progress of a reaction.
Similar to the action of chemical catalysts, enzym~s are said to reduc~
Action the ma ni de of activ For example, activation energy for
aci sis O siicro moJ-1, while the activation energy is
o moi- . whe
1 . ythe enzyme, sucrase. Mechanism
for e enzyme a.cti~n has been discussed in Unit 5. t..®t , __.._,
. . "'t.. ___L ·_ Vtt" • y .
'Vitamins It has been obse_ ived tha,t .. ~ :,::-_;...;~... , s are required. in
small amounts in our diet bu · diseases . .
The.s e compounds ~e Cl}!_~ g ~ ~ ~
· ~ thesised in our b y t !ants SYI_!thesis _
so they areconsidereclase~~Qw.:tr-t1: -o ac ors. o , e ac ena
~ e. gul dirf produce spme oi ttii vffiifirlhs required by us. All the
vitamins are generally available in our dtet. Different vitamins belong
to various chemicai classes and it is difficult to define them, on the
basis of structure. They are genera.qy regarded as organic compounds
r~quired in the diet in sin~ i · 1amounts to perform specific
biological functions for: normal m~tenance of optimum growth
r4§1 Biomolecules
and health or the organl1m. Vitamins are designated by alphabete
A, B, C, D, et :;;.-,,-~..: em, are further
am~.ia.;_1 -groups e.g. 8
B2, Be, B12, et of vitamins Is d vlta.mtn u(
8
!ttould not b ;__7!1'Yt _riff.,. out the
- -- ....
• · ltam _..__,...-~__,~ ,c
fu.-- -~UI C
ili , wd
d days. as
~.l Vitamins are classtfled into two groups depending upon ilietr solubUtt},
Cla..lftcation of · fat.
Vitamin, vttamtns: Vitamins which are soluble in fat an Us
e in water ar D.l..,l.w.1-J'il •
Th
inwa
be su
urine · ·
&m
ilietr deficiency are listed ·
.d .-!-\-tl~ tf\ P.t\ff' -Pi~ mat\ th ·
-../!)~ e 14.3: _Some important Vitamins, their ~ ources and th~ir
v'fieficiency Disea1es -
1 I {
in Yeast, milk, egg yolk, ConV1,1lsions
cereals ~~:. grams
-
ll\1,-.
B12
,. , ,. ., ,. -·--
Meat, fish, egg and
curd
Pernicious anaemia
e icient
haemoglobin)
In
Exposure to sunlight,
Chemistry t4:2f ·
1
ltarntn E lke whe l._l.,,IJ,U.;.I~• d of
0 .,~ ower oi an - ..-. lar
14.5.1 Chemical Complete hydrolysis of DNA {or RNA) yields a pentose sugar, phosphoric
Composition acid and nitrogen containing h~terocyclic compounds {called bases). In_
of Nucleic DNA molecules, ~ ~ gar moiety is ~-D-2-deoxyrtbose whereas in
Acids RNA molecule, it is_,, - -rtbose.
5 .
HOH2C O 0
OH OH OH H
/3-D-rtbose /3-0-2-deoxyrtbos.e
dW..!i Biomolecules
/
DNA contains four bases vtz. adenine (A}, guanine (G), cytosine (C)
and thymine m. RNA also contains four bases, the first thre~ bases are
same as In DNA but the fourth one Is uracil (U).
NH2
I
ho)
H'\r ~CH
»<;&NH,
Guanine· (G)
c·,
H3 ?i
C
'c/. .'NH
11 1 ·
HC~ ~O
H
Thymine m Uracil (UJ .
14.5.2 Structure A unit fo11I1ed ·b the attac,hment of a base to 1' position of sugar is
.of Nucleic . known ucleosi In nucleosides, the sugar carbons ate nwnberect
Acids as l', ', ', . in or~er to distingui_sh these from the bases
· {Fig.14.5a). When nucleoside is linked to phosphoric acid at 5'-position
of sugar moiety, we geta nucleotide (Fig. 14:5).
0- r-
n
o-
5•
"""f½C .
OH
Chemistry ~
_ Phosphodtester
linkage
. OH
3, end of chain
~ n of a dinucleottde
+T
- , · "Base
- i
Sugar - .
Pl\osphate Sugar- Phosphate l_
n SugarJ I-
lnfonnation regarding the sequence of nucleotides in the chain
. of a nucleic · · ailed its primary structure. Nucleic acids
have se.~~&,,........... s e also. James Wat~on and Francis Crick
gave a an helix structure for DNA (Fig .. 14. 7). Two . I
nucleic acid chains are wound about each other and ·held together .
by hydrogen bonds between pairs of bases. The two strands are
complementary' to .each other because the hydrogen bonds are
formed between specific pairs of bases. Adenine forms hydrogen
bonds With thymine whereas cytosine forms hydrogen bonds
With guanine.
In s~ond structure of RNA, helices are resent which are
only sin e stranded. Sometimes ey fold ack on themselves to
orm a double heUx .structure. RNA molecules are of three types
and they perform different fun~tions. They are named as messenger ·
RNA (m'.'RNA), ribosomal RNA (r-RNA) and transfer RNA
(~·RNA). . .
t4WJ 6iom01w1J,....e,...s____ _
Har Goblnd Khorana
Har Gobind Khorana, was born in 1922. He obtained his M,Sc
degree from Punjab University in Lahore. He worked with Profe880;
Vladimir Prelog, who moulded Khorana's thought and philosoph
towards science, work and effort. After a brief stay in India
1949, Khorana went back to England and -worked with Profes~or
O.W. Kenner and Professor A.R.Todd. It was at Cambridge, U.I{
that he got interested 1n both proteins IUJ!~~cletc acids. Dr Khorana shared the
Nobel Prize for Medicine and Ph s · 1968 with Marshatf Nlrenber and ~ii'"'"-
r~t:
JPWfo identify the dead bodies in any accident by comparing the DNA's of parents or
14.5.3 Biological DNA is the chemical basis of heredity'and mafbe regarded as the reserve .
Flinctlon1 of genetic information. DNA is exclusively responsible for maintaining
of Nucleic the identity· of different species of organisms-over milliqn~ of.years. A
Acid.a DNAmolecule·is capable of self duplication d~g_cell division 8.Ild
id_entlcal DNA s~d§ are transferred to daughter cells.-Another important
function ofnucleic acids is the protein synthesis in the cell. Actually, the
proteins are synthesised by various RNA mole~ules in the cell but the
. message for the synthesis of a particular protein is present in DNA
14.6 '11,ormo_nes · Hormone~ are molecules that act as 11?,tercell:ular messengers. These
are produced by eridoc~e glands in_the body and are_poured_directly
· in' the blood stream which transports them to the site of actfon.
In terms of chemical nature, some of these~ steroid~gens
s; so~5-•are poly pe';8e.!3 for e x a m ~}and
d....some others , arend acid derivatives such as
d norepinephrine. .
Hormones have several functions in the body. They help to maintain
the balance of biological activitles.in°the'body. The role ·o f insulin.in keeping
the blood glucos~ level within the .narrow limit is example qf this .
function. Ir?.sulin,is released in response to the rapid rtse in blood glucose
level. On the other hand hormone glucagon tends to increase the glucose
' level in the blood. The two hormones together regulate,the glucos~ level
in the blood. Epinephrine and n,orepinephrine mediate responses -to
external stimuli. Growth hormones and sexhormones play role in growth
and development. Thyroxine produced in the th id
derivative of amino aci ~ osine. normally low level of thyroxine leads
Chemistry 1;4 3..£i:•
s-and obesity,
to hYPothyrold1s m which Is ch arac terised by lelh a rgyi:C: 1evel of iodine
Increased level of thyroxJne causes hyperth yroidis m . ent of the thyroid
ln the diet m ay lead to hy pothyroidis m a nd e nlarge~lng sodium iodide
gland . Th ltlon Is la rgely being controlled by a
to ble s alt " " s
ln~~~;;;.,....;.:e,;;;~~:.:;.;~ e,
pl nc etaboll~m. modulat';,.,
~~cocorttcoids control the carbohydrate m ti s to tress. Toe
u ulanunato r are involved in reac on e
e eve o excretion of water anof the results
none
• a en cortex does not function pr a wes).kness and
may b e Addison's characterised by h es~ it is treated 1>Y
"fil,[w;~~~~~.;;;,=:~:..:;~ ess. The disease,,___ , ed by gonads are
;;;~ ~~~~~!!;!.~~~~ o!::::
co~rtl
~ coids. Ho h ters Testosterone is
th t of secondary sex c arac ibl~ for development
e lllajor sex hormone produced in males. It is respons •ral physical
of secondary male characteristics (deep voice, faci~ hair, g~1: responsible
constttutton) anc;i estradiol is the main female sex honnC::d artlcipates in
for development of secondary female charactertatlcs bl p for preparing
the control of menstrual cycle. Progesterone is responsi e
the uterus for implantation offertilised egg.
Summary_
Carbohydrates .are optically active polyhydroxy aldehydes or ketones or molecules which
provide such units on hydrolysis. They are broadly classified into three groups -
monoaaccharides, dlsacchartc:iea and polysaccharides. Glucose; the most important
. I
source of energy for mammals, is obtained by the digestion of starch: Monosacchartdes
are held together by glycosidic linkages to form disacchartdes or polysaccharides.
Proteins are the polymers of about twenty differe~t a-amino acids which are
linked by peptide bonds . Ten amino acids are ·call~d essential. amino acids because
, they cannot be synthesised by our body, hence must be provided through diet. Proteins
perform· various structural and · dynamic functions in the organisms. Proteins which
contain only ex-amino acids are caJled simple proteins. The secondary or· tertiary
structure of proteins get disturl:ied on ·change of pH ot temperature and they are not
able to perform their functions. This .is called denaturatlon of proteins. Enzymes are
biocatalysts which speed up the reactions in biosystems. They are very specific and
selective in their. action and chemically all enzymes are proteins.
. Vitamins are ,accessory food fac.t ors required in the diet. -They are classified as
fat soluble (A, D, E and K) and water soluble (B group and C). Deficiency of Vitamins
leads _to many diseases.
. _Biomolecules __