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
Less prey means less predatoors
The nucleus is missing in a mature RBC
Answer:
Submergent plants are totally submerged, with all parts growing under water. Floating plants are not rooted like emergent or submergent plants. They float along the water's surface instead.
Explanation:
Diffusion occurs in all states of matter: solid, liquid, and gas. It occurs rapidly enough to be observable in a reasonable period of time, however, only in liquids and gases.