Answer:
Answer D
Explanation:
Unlike the gain or loss of member through immigration, emigration, or death, the age of a population's members does not effect population size, meaning the correct answer is D.
Answer:
c) It introduces a premature stop codon into the mRNA
Explanation:
Nonsense mutation is a type of point mutation (single nucleotide base is changed) which leads to premature stop codon. Stop codons are also called nonsense codons and that is way this type of mutation is called nonsense mutation. As a consequence, synthesized protein is incomplete and shorter than it should be (truncated protein), usually nonfunctional.
<h2>Functions of elbow joint </h2>
Explanation:
- The elbow joint should be rotated laterally.
- This is because the elbow is basically a pivoted joint, however, it has the extraordinary capacity to turn the distal arm in pronation and supination
- These exceptional movements, alongside a wide scope of dynamic exertional powers, incline the elbow and its structures to critical wounds, especially with tedious movements
- Understanding the life systems and the physical powers of development will help in diagnosis
- Hence, the right answer is "elbow joint should be rotated laterally on an (AP), when the radial head is slightly superimposed over the proximal ulna on the first effort"
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.
