Hybridoma cells immobilized on surfaces of Sephadex beads are used in a packed column for production of monoclonoal antibodies (Mab). Hybridoma concentration is approximately X = 5 g/l in the bed. The flow rate of the synthetic medium and glucose concentration are Q = 2 l/h and S0 = 40 g/l, respectively. The rate constant for Mab formation is k = 1 gX/l-d. Assume that there are no diffusion limitations and glucose is the rate limiting nutrient.  If Yp/s is 4 mg Mab/g glu, determine the effluent Mab concentration of the system?

#Question id: 711

#Part-B Specialized Branches in Biotechnology

The shortest alpha helix segment in a protein that will span a membrane bilayer has about.

#Question id: 713

#Part-B Specialized Branches in Biotechnology

Which of the following polypeptides is most likely to form an α helix?

#Question id: 715

#Part-B Specialized Branches in Biotechnology

A protein is made up of 200 amino acids with alpha helix region containing 100 amino acid residues and 80 amino acids making antiparallel beta sheet and rest 20 amino acids in extended form. What will be the total length of this protein?

#Question id: 717

#Part-B Specialized Branches in Biotechnology

What is Φ & Ψ angles for collagen triple helix?

#Question id: 719

#Part-B Specialized Branches in Biotechnology

Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?

#Question id: 721

#Part-B Specialized Branches in Biotechnology

Addition of urea leads to a two-state transition between α-helix and random coil conformation. It has been observed that [θ]222 of the polypeptide is -11000 deg cm2 dmol-1 in the presence of 6M urea. Initially it was observed that tile values of mean residue ellipticity at 220 nm ([θ]220) are -36000, and +4000 deg cm2 dmol-1 for α-helix, and random coil conformations of this polypeptide. The percentage of the polypeptide in α-helix conformation is: