You are on page 1of 1

DEPARTMENT OF BIOCHEMICAL ENGINEERING AND BIOTECHNOLOGY

Maior .~xalllination
BEL311: Physicaland ChemicalI'n)pcrtiesof Biom?lecules
Max. Marks: 45 Time: 2 hom',

/Jr(,l'itJ'is the soul (~lcommuJ1icatiol1. E.xtralleOllS il?fiJrnwtion will he pellalized!

I. Show that the wavelength of the emitted photons cannot be longer than the wavelength of t'te cxeitaliull
photons Il)1a Iluorophore.
It i
2. Given a microbial cell. provide a protocol (in form of a flow diagram/table) to purify intraccllul:,:
proteins. What would be tbe major difference in the methodology for purifying membrane proteili
Clearly mark the sleps in the t1ow diagramltable for answering the latter.
(4.j:~ :
3. What is thc Iluid-mosaic modd It)[biologicalmembrancs'?What are memhrtme rails? Whal hiocltcll1i..
and hi(Iphysical experimental evidence den}onstratcsthe presenceor membrane raIts.
(2 +:2 -1.1 )j
4. Biomolccular asymmetry is an inherent feature of biological membranes. \-vhen they ::n~a part of a livil1!'
system. List the asymmetries. Why are these asymmetries abs,.;;nt in syntheti!:~ systems (;'.g. liposol1ll:s\ '
(4 +.~ j, I

5. Nam<:the Wl.:akand strong interactions of biolllo\ecuies. Why is it import:!:;: that v,::'" illteractiolh. P' 'f
Slrolig (lm~s.mediate biomolecular interactions including recognition'?
(4.j ~ (:

(), What ;IIT the limitations of SDS-PAGE? Why does one require a cross::ilkl'r 10 i.kllt;:\' I)fiJI"1I1
L'OIl1j1k"l'S hy SDS-PAGE'?
!.? f 21'
7, J\ microlll' having biological membranes of thickncss of I nlll has been di'-:l"c)VC]"!i, \ (ltal !n!!; II!
analyscs l'wlII that microbe reveal the same components for protein ttmlwticn as di~';" '\ ':1 vd in g\.lIl'i ,d
till date. It i:; hypothesized that protein folding in the microbelt)IlO\vs the sam(' gelll:rai principles tl1;)1
are \Vcll ;lCCl'ptcd so far. Analysis or the whole c(:lllysatL' rcsul\/:d in a large aliHillnt ot";\ 1(1\\ Ilwkctil:'

""eight .'.(X.5 KD3Q !~~~in


!S:1.hL~j~\)laI~tt~~~,)yl!()t~l~4>Il~/v,
(us\.' the hydr:')rrl~)bicltyscale pro\tided below):
t ISeq~lencing could ren:;:! only a porlion
Answerthe following qucstiol1srcg:mlinL~thc prolt';I:
of the protein a'.

,S if (a) How many amino acid residues ,:'ould be expected.in the ~ltllprotein?
~ (:) t (b) I\()\v n~any transmembrane dOI~lallls. docs the protell1 ~i~ve?
I . r.cr~ (c) :X-s~umlJ1gthat the values prov.lded III the hydror:hob!clty sca\c bd{)\\' .represent ~l1alll "
( () G~' In free energy, what can be saId ahout the expertmeptallsyslem used lo!' gcneratlllt: 111
I' C) 61, scale?
(: () 6~ 61 Y r L L-I+- -; I
(2 I 7 + .2 Ii
I' ,~
~
~biCitY scale given by Eisenberg et aI., j, Mol. BioI. (1984): t' I
;\ J{ "
., () (' E () (j II I I K I'd F I' " \\ )

II (,2 -:!.-;; .11iX -II" 1119 -o.XS -0.74 0.-18 -0.4 UX 1.01, -15
.-
0.6-1 I 1'1 O.!2 .11.IX -/111'; IIXI II 2/,

~( .co'7 r. ~.l) 1/f~


tJ' % ./ O (,1u b.o tJ1' ~1-6r1f2-
. 'b~ '5' g~~
l d~~
' .J I. ,~ /
"
r;.. rf',t..
~
?1
1.11J'
/"J ;"', '3 /IV
b C- tl'
~O ~/1t1 II

cJt?Vf' ~k'o ~.4.1


1~ -1,.£) I ,f
~
~ . 19.8
- 0'b? P ~.
,"
) . ftJ n
h I" /1'6, "'-/6 'I
0-. ..-0,18
0,2'
-o,oS'
'~~X- ,-0 , '(

\;;:[ - ~ ~
--- .~~~.

You might also like