Scribd
Upload
77 views2 pages

Mid-Sem 2016

The document is a mid-semester examination for a biophysics course consisting of 13 questions testing concepts related to molecular structures, energies, forces, and properties. The questions cover topics such as bond orders, molecular interactions, DNA melting temperatures, polymer properties, protein folding, and amino acid properties.

Uploaded by

SPyDeR 156
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
77 views2 pages

Mid-Sem 2016

The document is a mid-semester examination for a biophysics course consisting of 13 questions testing concepts related to molecular structures, energies, forces, and properties. The questions cover topics such as bond orders, molecular interactions, DNA melting temperatures, polymer properties, protein folding, and amino acid properties.

Uploaded by

SPyDeR 156
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
You are on page 1/ 2

Department of Physics

Indian Institute of Technology Kharagpur


Kharagpur-721302, West Bengal, India

Subject No. PH60402 (BIOPHYSICS)


Tuesday 23rd February, 2016
Duration : 2 Hrs; Total Marks: 20
Mid-Spring Semester Examination-2016
NOTE: Questions from 1 to 9 carry ONE mark, question 10 to 12 carries TWO marks each, question 13
carry FIVE marks (each HALF).

§1. Find out the bond order of O2+ by drawing energy levels.

§2. Draw orientational dependences of covalent, hydrogen and van der Waal bonds and also mention the
strength of these bonds in kT unit.

§3. Define DNA melting temperature. Show through a graph.

§4. Write twisting and writhing number for a plasmid shown in Fig. A & B. (Given: ∆Lk =-2)

§5. Define number, weight and z-average molecular mass and show M̄n ≤ M̄w ≤ M̄z .

§6. Mention the level of structures for amino acid and nucleic acid.

§7. Estimate the radius of gyration (Rg ) of a linear Gaussian chain having N number of monomer and
each monomer has length b .

§8. Define shape factor. Calculate the shape factor for spherical micelles.

§9. Estimate the dipole moment for the charge distributions (Q, -2Q, Q) shown in figure. All values are
in SI units. Does the result depends on the frame of reference?

§10. A double stranded DNA is pulled end to end under a ramped force upto 150 pN. What are the energy
contribution in this extended worm-like chain model? Draw Force-Extension curve for unzipping of
dsDNA. (label the axis clearly and all transitions)

§11. Estimate the height from the Earth surface where probability for O2 molecule is 1/e at 25 0
C.
2 −23
Comment on your answer. (take g=9.8 m/s as constant value upto this height; kB =1.38×10 (SI
unit))
Biophysics (PH60402) 2

§12. The end-to-end distance of a biopolymer is given as


h  i
l
2
< R (l) >= 2 L2p Lp
− 1 + exp − Llp
and radius of gyration is given by
RL RL
< Rg2 >= 1
L2 0
dl l0
dl0 < R2 (l − l0 ) >

Show that the radius of gyration for a rod like polymer (where Lp >> L ) will be L2 /12.

§13. Answer following questions

(a) For attractive potential like − rCn , where C is a constant and n is an integer. The value of n for
total interaction with other molecules (very small size molecule) would be

i. 1 ii. 2 iii. 3 iv. 4


(b) Pitch of α− helix in a protein is

i. 3.4 Å ii. 2.4 Å iii. 5.4 Å iv. 6.4 Å


(c) The stiffness (C∞ ) of a polymer is 3. The freeness of the monomer would be
√
i. 1/3 ii. 1/2 iii. 3/2 iv. 1
(d) Which one is protein misfolding disease

i. Tuberculosis ii. Cholera iii. Hepatitis iv. Type II diabetes


(e) Which of the following may be the value for persistence length of a protein

i. 0.3 nm ii. 1 nm iii. 2 nm iv. 50 nm


(f) The Madelung constant for 1D crystal where positive & negative ions are separated by 5 Å is

i. 1.87 ii. 1.74 iii. 1.61 iv. 1.38


(g) A protein consist of 51 amino acid and each residue can have 3 different conformations. This
protein fold into one native state. The change in the conformational entropy (at 27 0 C) of this
protein folding is

i. 50 kB ln (3) ii. 25 kB ln (2) iii. 1500 kB ln (3) iv. 300 kB ln (3)


(h) Empirically estimate the folding time (in µs) for a single domain protein having 100 amino acids

i. 1 ii. 1.5 iii. 2 iv. 3


(i) Isoelectric point of an amino acid having pK1 =2, pKR =4, pK2 =9 is

i. 8 ii. 6.5 iii. 5.5 iv. 3


(j) Which amino acid absorbs ultra-violet light?

i. Tyrosine ii. Glycine iii. Alanine iv. Cysteine

You might also like