kid form:
Prokaryotic cells use binary fission, a process by which a single cell splits into two cells to multiply. Since binary fission makes exact copies of the parent cell, this doesn't wants me to put in the rest of the information
next form:
In the process of binary fission, an organism duplicates its genetic material, or deoxyribonucleic acid (DNA), and then divides into two parts (cytokinesis), with each new organism receiving one copy of DNA. ... Binary fission is the primary method of reproduction of prokaryotic organisms.
<span>Eutrophication or more precisely hypertrophication, is the enrichment of a water body with nutrients, usually with an excess amount of nutrients. This process induces growth of plants and algae and due to the biomass .... Although eutrophication is commonly caused by human activities, it can also be a natural process, ...</span><span>
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The answer is North Pacific Gyre, just took the test. :)
Answer:
Part A - Increases the mechanical strength of protein
Part B - Disulfide bonds in the BPTI cysteines residues prevent protein from changing its structure and form
Explanation:
Remaining part of question
Part B
Most globular proteins are denatured and lose their activity when briefly heated to 65 degree C. However, globular proteins that contain multiple disulfide bonds often must be heated longer at higher temperatures to denature them. One such protein is bovine pancreatic trypsin inhibitor (BPTI), which has 58 amino acid residues in a single chain and contains three disulfide bonds. On cooling a solution of denatured BPTI, the activity of the protein is restored. What is the molecular basis for this property?
Solution
Part A
Disulfide bonds are covalent bonds which are much stronger than the non-covalent forces in protein i.e hydrogen bonds, weak wander vaal forces etc. Being strong in nature, the disulfide bonds causes cross linking between the chains of protein. This cross linking develops strong bonds that enhance the stiffness and hardness of the protein thereby increasing its mechanical strength. Stability increases because the entropy decreases.
Part B
The disulfide bonds with in the BPTI’s three adjacent cysteines, prevents the protein from changing its structure to any stable form and hence prevent it from folding and unfolding completely
