TLS Online TPP Program

#Question id: 108


Like plasmologens, sphingolipids are found in relative abundance in

#Biochemistry
  1. bacteria.

  2. plant cells.

  3. nerve cells.

  4. intestinal cells.

More Questions
TLS Online TPP Program

#Question id: 40229

#Applied Microbiology

Assertion (A): Photosynthetic bacteria like Rhodobacter can fix atmospheric nitrogen.

Reason (R): These bacteria possess the nitrogenase enzyme complex, which is sensitive to oxygen.

TLS Online TPP Program

#Question id: 40230

#Applied Microbiology

Match the specialized structures/enzymes with the corresponding nitrogen fixer:

List-I (Structure/Enzyme)List-II (Microorganism)
(A). Heterocyst(I). Rhizobium
(B). Leghaemoglobin(II). Anabaena
(C). Respiratory Protection(III). Clostridium
(D). Anaerobic N-fixation(IV). Azotobacter

TLS Online TPP Program

#Question id: 40231

#Botany

Match List-I with List-II

LIST-I (Plant Name)LIST-II (Family)
A. Arachis hypogaea (Groundnut)I. Pedaliaceae
B. Sesamum indicum (Sesame)II. Malvaceae
C. Linum usitatissimum (Flax)III. Fabaceae
D. Gossypium hirsutum (Cotton)IV. Linaceae
Choose the correct answer from the options given below:

TLS Online TPP Program

#Question id: 40232

#Applied Microbiology

In SDS-PAGE, which of the following reagents is specifically responsible for unfolding the tertiary structure of proteins by coating them with a uniform negative charge?

TLS Online TPP Program

#Question id: 40233

#Applied Microbiology

Consider the following statements regarding vertical gel electrophoresis (SDS-PAGE):

Statement I: The separation of proteins in SDS-PAGE is primarily based on their intrinsic isoelectric point (pI).

Statement II: Dithiothreitol (DTT) can be used as an alternative to beta-mercaptoethanol to achieve protein reduction.

TLS Online TPP Program

#Question id: 40234

#Applied Microbiology

Assertion (A): In the absence of beta-mercaptoethanol, a multimeric protein linked by disulfide bridges will migrate as a single large band.

Reason (R): beta-mercaptoethanol acts by oxidizing the thiol groups of cysteine residues to form stable covalent bonds.