The data from anchoring the protein complexes into the membrane tells that there is no spacial difference between the converged area per lipid values (table1). In addition, there is a higher delta g binding in the mutated protein compared to the normal protein(table 2,3). Another difference includes the delta g total was higher in the mutated protein compared to the normal proteins (table 2,3). The results of the experiment also showed that residue 16 was crucial for changes that are induced by the mutation, and both of the mutations alter the structure and the interaction of the proteins by changing the binding properties. In the PCA, it’s revealed that PMP L16P hsd more negative eigenvalues on the first PC and PMP22 T118M had a more positive eigenvalue (figure 2). Revealing that the mutants are more flexible compared to that of the mon mutated protein, which suggests a higher number of conformational states. The data that the mutated system is more flexible is supported by the data that the mutated systems have are less stable than the normal protein. The PCA also showed that the highest fluctuation was concentrated along the alpha helix 3 loop and the alpha-helix 4 loop in normal protein and in the mutated protein, the fluctuation was highest at lppo alpha-helix 1-2. In both of the mutations, there was a reduced number of hydrophobic contact and less hydrogen bond around the mutated parts of the protein (figure 2,4,5). The mutated complexes also have a higher delta g binding, leading to the inability of the protein to leave the ER(table3).
Recent comments