#Question id: 24133
#Part-A Aptitude & General Biotechnology
#Question id: 627
#Part-A Aptitude & General Biotechnology
Which of the following is correct ‘Dixon Plot’ for competitive inhibition for enzymes
#Question id: 4813
#Part-A Aptitude & General Biotechnology
You perform the three different two-factor crosses (Cross 1: XY and xy, Cross 2: YZ and yz, and Cross 3: XZ and xz). Assume all crosses are between diploid flies homozygous for the alleles of these genes. You observe 7% recombinants in the first cross, 20% recombinants in the second cross, and 13% recombinants in the third cross. if cross between XyZ and xYz leads to which of the followining recombinant with double cross over .
#Question id: 373
#Part-A Aptitude & General Biotechnology
What is the hydroxyl ion (OH-) concentration of a solution of pH 8?
#Question id: 723
#Part-B Specialized Branches in Biotechnology
Common structural elements in proteins such as α-helices or β-sheets are characterized by uniformly repeating, energetically favorable main chain conformations which additionally exhibit a completely saturated hydrogen-bonding network of the main chain NH and CO groups. Although polyproline or polyglycine type II helices (PPII or PGII ) are frequently found in proteins, they are not considered as equivalent secondary structure elements. Which of the following statements are correct about PP and PGs.
A. PGII -like helices form hexagonal bundles which appear to fulfill the criterion of a (largely) saturated hydrogen-bonding network of the main-chain groups
B. main chain NH and CO groups of the central PGII -helix are saturated by either intra- or intermolecular hydrogen-bonds, resulting in a self-contained hydrogen-bonding network
C. The formation of the right-handed PPI helix is possible only with proline residues because of the required cis conformation.
D. PPII helices seem to be stabilized by main chain-water hydrogen bonds (in the absence of main chain- main chain H-bonds), and tend to have a regular pattern of hydrogen bonds with water. After this, it is not surprising, that PPII helices are found mostly on the protein surface.