When atoms in a covalent bond share electrons unequally (one atoms pulls more than the other), the bond is said to be a polar bond is formed when electrons are unequally shared between two atoms. Polar covalent bonding occurs because one atom has a stronger affinity for electrons than the other (yet not enough to pull the electrons away completely and form an ion).
Answer:
Cells in a large multicellular organism communicate with each other by chemical signals. These signals are passed from one cell to another. To receive and respond to a chemical signal, a cell must have a <u><em>receptor</em></u> for that chemical.
Explanation:
To generate a physiological response, all cells in the body have special proteins called receptors. These receptors are involved in detecting a chemical signal and generating a response. The receptors are specific for different kind of chemical signals. For example, a dopamine receptor will bind a dopamine molecule whereas an insulin receptor will be able to bind an insulin molecule. Apart from chemical signals, some cells might also respond to mechanical signals.
Answer:
2
Explanation:
because it being pressure
Since a fox has a backbone and all to be a vertebrate you must have a backbone then a fox is a vertebrate.
Hope this helps!
Can u plz mark me as brainliest? I really need it!
Answer:
The options A, B, and D are all valid.
Explanation:
- The reason is that some proteins require molecular chaperones if they are to fold properly within the environment of the cell. In the absence of chaperones, a partially folded polypeptide chain has exposed amino acids that can form non-covalent bonds with other regions of the protein itself and with other proteins, thus causing nonspecific aggregation of proteins.
- The option A) is correct because the protein you are expressing in bacteria is being made in large quantities, it is possible that there are not enough chaperone molecules in the bacterium to fold the protein. Expressing the protein at lower levels might increase the amount of properly folded protein.
- The option B) is correct as urea should solubilize the protein and completely unfold it. Removing the urea slowly and gradually often allows the protein to refold. Presumably, under less crowded conditions, the protein should be able to refold into its proper conformation.
- The option C) is not correct as treating the aggregate with a protease, which cleaves peptide bonds, will probably solubilize the protein by trimming it into pieces that do not interact as strongly with one another; however, chopping up the protein will also destroy its enzymatic activity.
- The option D) is correct because overexpressing chaperone proteins might increase the amount of properly folded protein.
- The option E) is not correct as heating can lead to the partial denaturation and aggregation of proteins to form a solid gelatinous mass, as when cooking an egg white, and rarely helps solubilize proteins.
