Take for example - you touching something sharp and instantly moving your hand away.
Sensory neurons in your fingers detect the external stimuli of the sharp object and send a nerve impulse to the spinal cord (does not reach brain) and is sent back to a motor neurone - attached to an effector that moves the muscle and moves the hand away. This is a rapid reflex action and involuntary.
The structure of a typical antibody molecule
Antibodies are the secreted form of the B-cell receptor. An antibody is identical to the B-cell receptor of the cell that secretes it except for a small portion of the C-terminus of the heavy-chain constant region. In the case of the B-cell receptor the C-terminus is a hydrophobic membrane-anchoring sequence, and in the case of antibody it is a hydrophilic sequence that allows secretion. Since they are soluble, and secreted in large quantities, antibodies are easily obtainable and easily studied. For this reason, most of what we know about the B-cell receptor comes from the study of antibodies.
Antibody molecules are roughly Y-shaped molecules consisting of three equal-sized portions, loosely connected by a flexible tether. Three schematic representations of antibody structure, which has been determined by X-ray crystallography, are shown in Fig. 3.1. The aim of this part of the chapter is to explain how this structure is formed and how it allows antibody molecules to carry out their dual tasks—binding on the one hand to a wide variety of antigens, and on the other hand to a limited number of effector molecules and cells. As we will see, each of these tasks is carried out by separable parts of the molecule. The two arms of the Y end in regions that vary between different antibody molecules, the V regions. These are involved in antigen binding, whereas the stem of the Y, or the C region, is far less variable and is the part that interacts with effector cells and molecules.
The answer is c. coccolithophore is a unicellular, eukaryotic phytoplankton
Answer:
Explanation:
During translation, ribosomal subunits assemble together like a sandwich on the strand of mRNA, where they proceed to attract tRNA molecules tethered to amino acids (circles). A long chain of amino acids emerges as the ribosome decodes the mRNA sequence into a polypeptide, or a new protein.
