Rot values are expressed in term of

TLS Online TPP Program

#Question id: 34114

#Unit 2. Cellular Organization

The tail of which histone/s is able to contact an H2A-H2B dimer in an adjacent nucleosome, which may contribute to the formation of higher order structures

TLS Online TPP Program

#Question id: 34115

#Unit 2. Cellular Organization

Choose correct statement

TLS Online TPP Program

#Question id: 34116

#Unit 2. Cellular Organization

A. The positive charge on lysine is neutralized upon acetylation

B. Methylated lysine and arginine are neutral.

C. Lysine can be mono-, di-, or triacetylated

D. Arginine can be mono or diacetylated. 

E. Both Lysine and Arg can be acetylated

Choose true and false

TLS Online TPP Program

#Question id: 34117

#Unit 2. Cellular Organization

A. In the solenoid model, the nucleosomal DNA forms a superhelix containing approximately six nucleosomes per turn

B. In the solenoid model, the linker DNA is buried in the center of the superhelix, but it passes through the axis.

C. Zigzag conformation requires the linker DNA to pass through the central axis of the fiber in a relatively straight form

D. Zigzag conformation the nucleosomal DNA forms a superhelix containing approximately four nucleosomes per turn

Which of the following is correct

TLS Online TPP Program

#Question id: 34118

#Unit 2. Cellular Organization

A. Trypsin treated core histones quickly forms 30-nm fibers

B. Core histones lacking their amino-terminal tails are incapable of forming 30-nm fibers

C. Interaction between the positively charged amino terminus of histone H4 and a negatively charged region of the histone-fold domain of histone H2A is particularly important for 30-nm fiber formation

D. H2A that interact with the H4 tail are conserved across many eukaryotic organisms but are not involved in DNA binding or formation of the histone octamer.

Choose true and false

TLS Online TPP Program

#Question id: 34119

#Unit 2. Cellular Organization

30-nm fiber forms loops of 40–90 kb that are held together at their bases by a proteinaceous structure referred to as the nuclear scaffold. These are stabilised by