TLS Online TPP Program

#Question id: 41054


Q. Consider heat flow across a biological tissue layer that behaves according to Fourier's law (𝑱𝒒=−𝒌𝜵𝑻). If the tissue undergoes a physiological change such that its thermal conductivity (𝒌) doubles, but the temperature gradient (𝜵𝑻) across the tissue is reduced to half of its original value, how will the new heat flux (𝑱𝒒′) compare to the initial heat flux (𝑱𝒒)?

#Unit 12. Biochemical Engineering
  1. The new heat flux will be twice the original (𝑱𝒒′=𝟐𝑱𝒒).
  2. The new heat flux will remain the same as the original (𝑱𝒒′=𝑱𝒒).
  3. The new heat flux will be half of the original (𝑱𝒒′=𝟎.𝟓𝑱𝒒).
  4. The new heat flux will be four times the original (𝑱𝒒′=𝟒𝑱𝒒).
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TLS Online TPP Program

#Question id: 12996

#Unit 1. Structure and Function of Biomolecules

Which of the following is incorrect regarding to α-helix
a) In the α helix, the first four NH groups and last four CO groups will normally lack backbone  hydrogen bonds.
b) the length of an amino acid in α-helix reduced almost 3 times than linear structure.
c) the frequent occurrence of Pro and Gly residues favour α-helix formation.
d) dihedral (ϕ and ψ) angle should be close to -57 and -47.

TLS Online TPP Program

#Question id: 12997

#Unit 1. Structure and Function of Biomolecules

Which of the given reason is correct to minimize the repulsion in an α-helix
a) positively charged amino acids are often found near the amino terminus of the helical segment
b) negatively charged amino acids are often found near the amino terminus of the helical segment
c) positively charged amino acids are often found near the C-terminus of the helical segment.
d) negatively charged amino acids are often found near the C-terminus of the helical segment.

TLS Online TPP Program

#Question id: 12998

#Unit 1. Structure and Function of Biomolecules

Match with appropriate bonding pattern

Helix typeHydrogen bonding
a. α-helix1. n, n+3
b. 310 helix2. n, n+5
c. π helix3. n, n+4

TLS Online TPP Program

#Question id: 12999

#Unit 1. Structure and Function of Biomolecules

Proline and glycine both disturb the symmetry of α-helix which of the following are true regarding to these two amino acids
a) proline changes the orientation of hetropolymeric α-helix hence proline can be placed only as 1st amino acid residue near to C-terminus 
b) proline changes the orientation of polymeric α-helix hence proline can be placed only as 1st amino acid residue near to N-terminus
c) glycine disrupts the heteropolymeric α-helix by changing the helicity.
d) homopolymer of proline and glycine can form stable helix. 

TLS Online TPP Program

#Question id: 13000

#Unit 1. Structure and Function of Biomolecules

Identify the correct statement regarding the structure


TLS Online TPP Program

#Question id: 13001

#Unit 1. Structure and Function of Biomolecules

Which of the following is incorrect 
a) antiparallel β sheets are frequently found and they are quite more stable because of more no. hydrogen bond presence and linear H bonding pattern.
b) antiparallel β sheets are frequently found and they are quite more stable because of more no. hydrogen bond presence and having distorted H bonding pattern.
c) parallel β sheets are relatively less stable and mostly found in core of protein.
d) parallel β sheets are relatively more stable and mostly found in core of protein.