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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-B Specialized Branches in 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: 850

#Part-B Specialized Branches in Biotechnology

The experimental inverse of protein structure prediction, has provided insights into protein folding and stability. Protein design attempts to construct an amino acid sequence that will form a structure such as a sandwich of β sheets or a bundle of α helices;
TLS Online TPP Program

#Question id: 852

#Part-B Specialized Branches in Biotechnology

.________ enzyme revealed the relation between the amino acid sequence of a protein and its conformation.
TLS Online TPP Program

#Question id: 854

#Part-B Specialized Branches in Biotechnology

Many conditions including type 2 diabetes, Alzheimer  disease, Huntington disease and parkinson disease are associated with the misfolding mechanism a soluble protein that is normally secreted from the cell is secreted in the missfold state and converted into an insoluble extracellular fibre the diseases are correctly referred to as
TLS Online TPP Program

#Question id: 857

#Part-B Specialized Branches in Biotechnology

The aggregation of nonpolar side chains in the interior of a protein is favored by
TLS Online TPP Program

#Question id: 859

#Part-B Specialized Branches in Biotechnology

Which one statement is incorrect about ATG genes;
TLS Online TPP Program

#Question id: 861

#Part-B Specialized Branches in Biotechnology

Alexander Varshavsky discovered, the half-lives of many cytoplasmic proteins vary with the identities of their N-terminal residues via the so-called N-end rule:-

A. Destabilizing N-terminal residues Asp, Arg, Leu, Lys, and Phe have half-lives of

i. Only 2 to 3 minutes,

B. Stabilizing N-terminal residues Ala, Gly, Met, Ser, Thr, and Val have half-lives of

ii. >10 hours in prokaryotes

iii. >20 hours in eukaryotes.