Answer:
Option B, Most communities never become completely stable
Explanation:
In an ecological succession, most of the species are unstable and they keep on changing continuously. The succession is primarily of two types –
a) Primary Succession – In this, community of species occur on a new habitat which had been never occupied earlier. Or it can be said that it is entirely a new habitat.
b) Secondary Succession – In this, community of species occur in a habitat where earlier life existed but it was disturbed or damaged by some environmental condition.
Hence , the correct answer is option B
The best answer should be B.
Apparatus in laboratories can be really dangerous, especially the ones which involves electricity.
As a student, he should not just wrap the cord with electric tape, as he might wrap them in a wrong way and possible could hurt himself. So A is not a good answer.
And for C, even though it is a great idea not to use the frayed cord hot plate, but he should also notify the teacher as that hot plate with frayed cord may be passed on and be used for the other students which may pose a risk to them.
And obviously, using the hot plate with frayed cord is super dangerous and he could possibly get electric shock. So D is the incorrect answer.
And it's only left to B, it right to notify the teacher so the teacher can actually either fix it themselves or they wouldn't pass on to other students to use it.
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
Answer:
False.
Explanation:
Hydrophilic molecules are transported through facilitated diffusion with the help of channel or membrane protein.
Camouflage and protective coloration hides the predator from it's prey and can also hide prey from predators because if they can't 'see' you, your chances of success and/or survival increase.
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