C. elegans embryo uses both autonomous and conditional modes of specification. Conditional specification at the 4-cell stage can be seen in the development of the endoderm cell lineage and also in the establishment of dorsal-ventral axis. Following are few statements regarding this figure:

A. If the P2 cell is removed at the early 4-cell stage, the EMS cell will divide into two MS cells and endoderm will be made.

B. In pop-1 deficient embryos, both EMS daughter cells become MS cells.

C. When the position of ABa and ABp was reversed, their fates get reversed and no normal embryo forms.

D. In embryos whose mother have mutant glp-1, ABp is transformed into ABa cell.

Which of the above statements are true?

#Question id: 887

#Unit 1. Molecules and their Interaction Relevant to Biology

Polypeptides fold rapidly by a stepwise process, how does the polypeptide chain arrive at its native conformation?

#Question id: 888

#Unit 1. Molecules and their Interaction Relevant to Biology

Which one of the following statements about the protein folding is incorrect?

#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?

#Question id: 890

#Unit 1. Molecules and their Interaction Relevant to Biology

Some of the misfolded protein or defective Protein causes disease as follows;

               Disease                                             Defective Protein

A)  Parkinson’s disease                                  i) Amyloid-β protein

B)  Alzheimer’s disease                                  ii) Superoxide dismutase

C) Huntington’s disease                                iii) Lysozyme

D) Lysozyme amyloidosis                             iv) α-Synuclein

E) Amyotrophic lateral sclerosis                   v) polyglutamate expansion

Match the correct disease with its misfolded proteins;

#Question id: 891

#Unit 1. Molecules and their Interaction Relevant to Biology

The folding pathways of some proteins require two enzymes that catalyze isomerization reactions such as,

a) Peptide prolyl isomerase (PPI)  catalyzes the elimination of folding intermediates with inappropriate disulfide cross-links

b) Protein disulfide isomerase (PDI) enzyme that catalyzes the interchange, or shuffling, of disulfide bonds until the bonds of the native conformation are formed

c) Peptide prolyl cis-trans isomerase (PPI) catalyzes the interconversion of the cis and trans isomers of Proline residue peptide bonds

d) Peptide prolyl isomerase (PPI) can be a fast step in the folding of proteins that contain some Pro peptide bonds in the cis conformation

Which of the following combinations is correct about protein folding pathways?

#Question id: 892

#Unit 1. Molecules and their Interaction Relevant to Biology

Assisted protein folding is mediated by a group of proteins known as chaperons, which of the following statements is incorrectly reperesents chaperon activity;