Answer:
one which is able to express itself outwardly in the presence of a recessive allele
Explanation:
Answer:
10 electrons
Explanation:
Normally you would assume the atom to be neutral, meaning the protons and electrons cancel each other, if nothing states the charge of the atom. So, there must be 10 electrons in order to cancel out the protons.
Hope this helped :]
Answer:
False
Explanation:
Rearrangements on introns and transposons usually don't cause severe consequences because those sequences are not part of coding genes and therefore cannot code for proteins, and if a rearrangement occur within a coding sequence of a gene might cause an incomplete and non-functional protein causing severe consequences to expression levels of that particular gene.
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.
