How was CSIR NET Exam Question paper?

90) We called proton ATPase means ATP will degrade or synthesize . in the case of flagella rotation it wont happen ,so we wont called proton ATPase . In the case of mitochondria or chloroplast or bacterial membrane where ATP synthesis that subunit only we  called proton ATPase .
and also i found many journals mutation of FLI G will show non motile ones.
for eg: Charged Residues of the Rotor Protein FliG Essential for Torque Generation in the Flagellar Motor of Escherichia coli
Scott A. Lloyd and David F. Blair*

The FliG protein of Escherichia coli is essential for assembly and function
of the flagellar motor. Certain mutations in FliG give a non-motile, or
Motÿ, phenotype, in which flagella are assembled but do not rotate. Mutations
with this property are clustered in a C-terminal segment of FliG
that is stable when expressed alone, and thus probably constitutes an
independently folded domain. Previously, we suggested that this domain
forms the rotor portion of the active site for torque generation in the
motor. In this work, we have used a mutational approach to identify the
amino acid residues in the C-terminal domain of FliG that are most important
for motor function. Site-directed mutagenesis was used to replace
each of the conserved residues in this domain with alanine, and the
effects on motor function were measured. Because charged residues have
often been suggested to have important roles in torque generation, conserved
charged residues were changed individually and in all pairwise
combinations. The results show that three charged residues of FliG,
Arg279, Asp286 and Asp287, are directly involved in torque generation.
Mutations in these residues cause motility defects that suggest that they
function jointly, in an active site whose most important property is a
speci®c arrangement of charges. Two other charged residues, Lys262 and
Arg295, may also be involved in torque generation, but are less critical
than Arg279, Asp286 or Asp287. Uncharged residues of the FliG motility
domain do not appear to have direct roles in torque generation, although
some are needed for the stability of the protein or for normal clockwise/
counter-clockwise switching. The Motÿ mutations of ¯iG isolated
previously by random mutagenesis do not alter the putative active-site
residues, but render the proteins abnormally susceptible to proteolysis,
suggesting signi®cantly altered conformations or reduced stabilities.

receptor 4 p53  means the element on DNA where p53 binds,,,,

the quest can be taken in 2 diff ways
1. which of the above are wrong statements? then the ans is 4 $5.
2. which of the above is the wrong step? then ans is 3to4. bcoz statement 3 is correct .and 4 is wrong. ie the mistake occur btn 3 and 4. rt? ie the wrong step is from 3 to 4.... clear ( in quest -which is wrong step)
 think about it..  part a for lifescience and maths are same.... all of their answer key tell it is 3.