BTECH- CS B205 1

PARAMM DALAL 100220001222

A
ASsIGNMENIL 3 S4 EB

(12DNA replication.

Ca) Initiation
In +hc replication complcx, cnzyme DNA helicasc
vnwinds dov blc hclix and breaks hydrogen_bonds
holding complemcntary bases o f DNA +0qcther.

Separation of 2 singi strandsd fDNA Creates

aty' shapc calleLd replicn fork2 stparatcd
strands will act as templatc for making new
strands of DNA.
Lea ding9
5 3
Lont
3 discont.
5
DNA Laggin
vnzips

DNA primasc is ancthcr cnzymc +hat is imp.

in bNA rEplicn, It synthesiz small RNA primer,
which act as kick - Starter"for DNA pOlymer-
asc

LbElongation -
Oncu DNA polymerase hasattachcdt o original
unzippcd istrands of DNA. it is ablc to Start
synthcsising new DNA +0match the tCmplatcs.
1closs tlme
 It cxtend the primer by addin4 frcc nucleo -

tides t0 3' end1

primer new DNA Strand
3.

3 DNA
polymcrase
oldRNA

Once dNA poly templaté is read in 3-s dir

which mLans, that ncw strand will bt formed
i n 5-3 dirr

AlongHhis it neLds to sunthesise RNA primer

only onc at beginning

RNA primer arc addLd to ncwly exposzd bascs

on laggina Strand 2 DNA Ssn: 0ccur in
fragmcnts. IhesL fraqments arc Okazaki.
3
5 TACA Cading
7
5 TT
DNA
3
ATGI ag4ing-
5

L Trmination
One bNA Syn has finishcd ncwlysyrthesised
Strands are bovnd and stabiliscd.
 With regard to lagging strand, 2 cnzymcs arc
nccded to achicve this RNA asc H that
removes RNA primcr prescnt at beginning of
okazaki. and DNA ligase that join fragments
+0gcther to creat onc cormput strand..

Following replich ncw DNA avtomatically

winds Vp into double helix

a DNA transcription-
cukaryotic

In euk.cell, multiplc RNA PolymcraSL arcreq

vnlike in prokaryotlc BeSids Lontrol scq.are
mvch CorMplicated in eUkaryotls.

Cytosot
DNA CUk

Transcription

ConscryLd stq that isclosest to start size of

ranscri ption is TATA box. It is Lentercd _at
pOsition-30. An initiatn Lomplex is formed in
b y transcrip n factors a t site before RNA Poly.

binds and transcripts.

0op

Start site
TATA
 When growing RNA chairs are only abt 30-
nucleo+idis along 5 ends by euk. ell prt mRNA
arc modificd addn_of mcthyl gaunin
Hriphosphat caps proccss Lalled capping.

Tney arL recogniscd by protcin factors involvCd

in_initlation_of +ranslation.
Incy protcct growing RNA chains from
dtgradation.
TELD
Scap crapp

TALA

Transcn procc.cds 1000-2000 nvclcoid beyond1

sitc that will beLom 3 terminals Tncn
distal_seqmcnt is removcd by cndonuclco -
tic clcavage.

nencnzyme poly CA) polymerasL add poly (aD

tails madc up of adcmylatc residucs to 3lcnd.
Inisc_cntrons are remavLd from RNA transcript
b RNA sVcing. Inis RNA is then transferrcd
+o yt0 p lasma for translatio1.

Lclass ime
 int-on 3 mRNA

Cxon RNA
SVCing 3 tait
5 LraPD 3
smaP
5' crapp
MCsSnger RNA

(3)Iranslation

It is process of translating sca of mRNA Mole

Lule to seq. of amino acids during protein
Synthcsisc GenctiLcodc describe relation bin
scq of base palrs in genc and amino acids.

STE PS

RibosoMc binds MRNA to spLcific area.

It Starts matching t RNA anticodons scq. to
MRNA cod ons.
Each iMc ncw t- RNA CoMcs into ribosom, thc
amino acids thatit was carrying gcts added
t0 polypep.
chain
Ribosomc continvcs vntilit hits stop se
Polypcp. forms into its native shape and starts
acting as funcn protcin inccll
4Michacl is- menton cqn significanLL of
kinctic pararMCters

I t is a satisfactory dcscrip n of kinctics of

manyitdustrial_enzymes, althovgh therearc
CxcepnSUch a qlucosL isomcrase.

Eqn is VE Vmax. Cs1

K4 Ls1

Vmax max vClocity achicycd by_sys. at

Max SU bstrate Lonc
Ku- SVbstrat Lonc at whic rcach velocity
iS 50/: of Vmax

Ls conc. of Substrat

Graphica lly Vmax

V
max

L5)Enzymc inhibition.
No. of Lomp_have ability t0 combinc with_certain
cnzymcs and block reacn, Svch Lomp. arz inhibi-
inhibition.
tors Proccss -
 Irreversible -
hcy are vSVallyconvalcntly bondcd to cnzymc
destroy funcna grovp in activL sidtMost of
irrey. inhib. are toxic.
cg pcnicilin act a s i r . inhibitor for
gycoprotcin_peptidasc.
RVcrsiblc
Inhib.dissociate from Lnzymc as former
non-LoValcnt bonding I+N enzymis
3 types are-

La) Cormpctitive
Structurc of this closcly resembles to that of
normal svbs bCLavsc_Of similar struture,
thcy bind to active side.

Lb)Non: Lomp.
Incy bind opp. t0 active sidc. Tnis binding
alters cnzymiS Lonformation and thcrcbs
blocks r n

Indy get attachCd to fret cnzume.

g Ag2t Hg2 ct
Uncompttitivc
Incs inhibitors combinc only Wth ES complCx
and not wlth frtc inzymis..
 I t isn'+ revcrscd by i n . svbstratt conc. It is
rate with single svbstrate and often fovnd
i n cnzymatic rcacn with 2_or more
Svbstrates

Lcass timo