TLS Online TPP Program

#Question id: 4188


In eukaryotes what is the function of eIF-4 (cap binding protein)?

#Unit 3. Fundamental Processes
  1. It assists in the dissociation of the ribosomal complex following termination of translation.

  2. It cleaves the first amino acid on a newly translated protein.

  3. It binds to the 5ʹ end of mRNA and assists in the formation of the pre-initiation complex.

  4. It acts as a general acid-base catalyst during the formation of the peptide bond.

More Questions
TLS Online TPP Program

#Question id: 4354

#Unit 3. Fundamental Processes

Which of the following statements correctly describes the primary difference between enhancers and proximal control elements?

TLS Online TPP Program

#Question id: 28804

#Unit 2. Cellular Organization

VASP is____
a)proline-rich
b)protect the end of the growing filament from CapZ
c)a pathogenic surface protein
d)involve to holding the end of the newly formed filament

Following are statements about VASP, except?

TLS Online TPP Program

#Question id: 4050

#Unit 3. Fundamental Processes

An antibody was produced and used in an immunohistochemical assay to detect the location of RNA polymerase II in a thin section of a liver biopsy. The section was stained with the antibody that had been labeled with a fluorescent tag, and then viewed under a fluorescent microscope. State where you would expect to find positive staining if the enzyme is present.

TLS Online TPP Program

#Question id: 889

#Unit 1. Molecules and their Interaction Relevant to Biology

The cis and trans GroEL rings undergo conformational changes in a reciprocating fashion, with events in one ring influencing events in the other ring. The entire GroEL/ES chaperonin complex functions as follows;

a) One GroEL ring that has bound 7 ATP also binds an improperly folded substrate protein, which associates with hydrophobic patches that line the inner wall of the GroEL chamber

b) The GroES cap then binds to the GroEL ring like a lid on a pot, inducing a conformational change in the resulting cis ring

c) Within ~10 s the cis ring catalyzes the hydrolysis of its 7 bound ATPs and releases the resulting Pi , which weakens the interactions binding GroES to GroEL

d) A second molecule of improperly folded substrate protein binds to the cis ring, followed by 7 ATP

e) The binding of substrate protein and ATP to the cis ring conformationally induces the trans ring to release its bound GroES, 7 ADP, and the presumably now better-folded substrate protein

Which of the following is incorrect functions of GroEL/ES chaperonin complex?

TLS Online TPP Program

#Question id: 28735

#Unit 2. Cellular Organization

Most common CFTR mutation is a ΔF508 causes_
a)Changing the conformation of the cytosolic portion of CFTR so that the signal is unable to bind to Sec24
b)Changing the conformation of the cytosolic portion of CFTR so that the signal is unable to bind to Sec23
c)blocking its packaging into COPII vesicles budding from the ER
d)blocking its packaging into COPI vesicles budding from the ER

Which of the following is correct result of mutated CFTR?