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TLS Online TPP Program
#Question id: 12998
#Section 2: General Biology
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
#Section 2: General Biology
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
#Section 2: General Biology
Identify the correct statement regarding the structure
TLS Online TPP Program
#Question id: 13001
#Section 2: General Biology
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: 13023
#Section 7: Recombinant DNA technology and Other Tools in Biotechnology
Which of the following enzymes are required for end labelling?
TLS Online TPP Program
#Question id: 13024
#Section 7: Recombinant DNA technology and Other Tools in Biotechnology
Inset and the vector can be ligated if they are digested by a pair of –