Molecular Switches

We live in the technical era. Almost everyone in the US has one computer or at least one computer. Most of the size of the computer you are accustomed to is about 7 "x 17" x 17 "This is a lot of space, these troublesome units will soon be replaced by small ones, Scientists have made significant research in studying its feasibility Our current technology consists of solid-state solid-state microelectronics.

There is also a need to strengthen information storage technology. For example it is possible to act as a molecular switch for molecular binary code. Molecular switches have the potential to reduce the storage capacity of information to one hundred thousandths and to reduce the storage speed of information by one million 3. Regarding ability, advancement of technology is also necessary. The nervous system - for example, lighting with the brain

Almost all molecular motors share common features: core ATPase domains that bind and hydrolyze ATP. It can switch between different conformations in a process similar to the GTPase molecular switch, but performs a protein scaffold very different. Bound to the core domain is a small mobile or translational domain that reads the core's nucleotide-dependent conformation and responds by conformational changes. These magnetic fields then convert the conformational change into a larger motion by changing the position of the amplifier region (usually lever arm or coiled coil). The position of the amplifier greatly changes with respect to the attached protein, and the protein eventually moves greatly (Fig. 3-17).

Figure 3-18 Structural and Functional Similarities between Different Molecular Switch Families In all of these figures, the position of the switch II helix is ​​indicated by the yellow color of the nucleoside diphosphate binding protein and the red is the triphosphate linkage Conformation is shown. The switch I region is schematically shown where the nucleotide gamma-phosphate is depicted as a red star. A specific polymer partner interacts with the switch region in both states and appears as a surface of the same color. The carboxy terminal helix of the ATPase or GTPase domain is shown in blue, to which the mechanical elements of the molecular motor or other domains of the G protein are bound. (A) Switching Region of Molecular Protein Kinesin II. Nucleotide driven conformational translocation in the kinesin switch II region causes a strong force in the neck domain (see Figure 3-17, not shown here), causing movement of the kinesin along the microtubule (MT) . . Sabrin Election