Which process allowed the nucleomorphs of chlorarachniophytes to be first reduced, and then (in a few species) lost altogether, without the loss of any genetic information?

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 type	Hydrogen bonding
a. α-helix	1. n, n+3
b. 310 helix	2. n, n+5
c. π helix	3. 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.

TLS Online TPP Program

#Question id: 823

#Unit 1. Structure and Function of Biomolecules

chaotropic agents such as guanidinium ion and urea, the efficiency of the chaotropic agent is measured in terms of-