This is the hydrophobicity plot of a novel protein isolated

This is the hydrophobicity plot of a novel protein isolated from C elegans. Based on this plot, how many transmemorane domains would you predict for this protein? Assume the membrane is 3 nm thick. The Y-axis of this graph shows the hydropathy index; DeltaG (non-polar solvent to H_2O) How many transmemorane domains would this protein most likely have if the Y-axis described the Delta G for transfer from H_2O to a hydrophobic solvent? 0 1 3 5 7 Which of the following transport steps in an intestinal epithelial cell can. under certain conditions, occur against a concentration gradient\' (uptake refers to \"into the cell\", export \"out of the cell\") uptake of glucose export of glucose uptake of Na^+ at the basolateral plasma membrane uptake of Na^+ at the apical plasma membrane export of K^+ Which of the following methods is most suitable to determine if the actin cytoskeleton is dynamic and constantly undergoes assembly and disassembly? Immunofluorescence microscopy with a primary antibody to G-actin(raisec in mouse) and a secondary anti mouse) and a secondary anti mouse antibody(raised in goats) coupled to a green fluoroprore. Live imaging of cells expressing GFP. tagged action FRAP analysis in cells expressing GFP tagged actin Electron miroscopy

Solution

1. Positive peaks indicate the degree of hydrophobicity and transmembrane helices.

So here the answer is 7 transmembrane helices .

Option E.

2. option E ie 7

The number of transmembrane helices in the protein shows the positive values for the free energy.

3. uptake of glucose.

After meal glucose concentration will be high in intestinal lumen and transport aginst concentration gradient to blood.

4. Live cell images of GFP-tagged actin.

5.cofilin binds to older actin filaments and destabilises actin.