DNA polymerase basically adds the nitrogenous bases to where they are needed on the strand. These work in a 5 prime to a 3 prime direction, and form okazaki fragments on the top strand.
Answer:
Explanation:
A. False - A symporter system requires that one of the molecules to be transported using passive transport.
B. True - The Na+ will move down the established concentration gradient releasing energy to facilitate movement of sucrose against its concentration gradient. This is known as secondary active transport.
C. False - sucrose moves through ion channels not by diffusion to better control its movement across the membrane.
D. True - Movement of molecules against their concentration gradient thus requiring energy input is known as active transport.
E. False - One of the molecules needs to be moving against its concentration gradient.
F. False - A Uniporter system allows the binding and transport of a single molecule at a time. A symporter allows simultaneous binding and transport of Na+ and sucrose molecules.
Answer:
sorry mate but thats wrong
Answer and Explanation:
Bovine pancreatic trypsin inhibitor (BPT I) is a small globular protein and it inhibits the proteolytic enzymes like trypsin. BPTI is composed of ∝ helices, β sheets and 3 disulfide bonds. Due to these BPTI is a stable protein in its tertiary structure. It is almost inert to denaturation by urea and exhibits denaturation below 100 degree, only in highly acidic solutions. When all the disulfide bonds in BPTI are reduced, the protein is unfolded at room temperature and can reform three correct S-S pairings in native confirmation. if the 6 cysteine residues are reduced and unfolded in urea, the re-oxidation would yield 3 pairs with probability of first pair with 5, second pair with 3 and the third pair with 1 cysteine residues. Therefore, 5 x 3 x 1 = 15 combinations are possible accounting for 7% of protein refolding.
