TLS Online TPP Program

#Question id: 887


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

#Part-A Aptitude & General Biotechnology
  1. proteins appear to fold in a hierarchical manner, with small local elements of structure forming and then to yield larger elements, which coalesce with other such elements to form yet larger elements and converted into its native conformation

  2. A protein-folding pathway has been highly successful in predicting the three-dimensional structure of small proteins from their amino acid sequence atleast 156 amino acid residue that have acquired their final structure

  3. Vander waal interaction play a significant role throughout the process, as the aggregation of nonpolar amino acid side chains provides an entropic stabilization to intermediates and, eventually, to the final folded structure

  4. The native conformation of the protein folding by stepwise manner such as unfolded→transition state→molten globule→folded conformation by decreasing the free energy

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TLS Online TPP Program

#Question id: 881

#Part-B Specialized Branches in Biotechnology

 ______and ________ are the first chaperones a newly made prokaryotic protein encounters. Subsequently, many partially folded proteins are handed off to other chaperones to complete the folding process. E. coli can tolerate the elimination of_______ or________, but not both, thereby indicating that they are functionally redundant.

TLS Online TPP Program

#Question id: 882

#Part-B Specialized Branches in Biotechnology

Choose correct statements about thermophilic proteins

I. The proteins found in thermophilic species are much more stable than their mesophilic counterparts.

II. All thermostable proteins have such a high incidence of salt bridges

III. the most important of which are an increased size of the protein’s hydrophobic core, an increased size of the interface between its domains and/or subunits, and a more tightly packed core as evidenced by a reduced surface-to-volume ratio.

IV. Several of these thermostable enzymes have a superabundance of salt bridges on their surfaces.

TLS Online TPP Program

#Question id: 882

#Part-A Aptitude & General Biotechnology

Choose correct statements about thermophilic proteins

I. The proteins found in thermophilic species are much more stable than their mesophilic counterparts.

II. All thermostable proteins have such a high incidence of salt bridges

III. the most important of which are an increased size of the protein’s hydrophobic core, an increased size of the interface between its domains and/or subunits, and a more tightly packed core as evidenced by a reduced surface-to-volume ratio.

IV. Several of these thermostable enzymes have a superabundance of salt bridges on their surfaces.

TLS Online TPP Program

#Question id: 887

#Part-B Specialized Branches in Biotechnology

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

TLS Online TPP Program

#Question id: 891

#Part-B Specialized Branches in Biotechnology

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?

TLS Online TPP Program

#Question id: 891

#Part-A Aptitude & General Biotechnology

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?