Answer:
Stratum Granulosum
Explanation:
The stratum granulosum is a layer of the epidermis and consists of four to six cell layers. The keratinocyte appearance changes in the cell layers of stratum granulosum as some cells stop dividing and the process of keratinization starts. Keratinization includes filling the cells with the protein keratin. During keratinization, the cells flatten, and the disintegration of their nuclei and organelles occur.
Due to the loss of the nucleus, these cells cannot divide and become dead. The keratinized cells accumulate keratohyalin granules and lamellar granules. The cells of this layer have thick plasma membrane due to the binding of cytosol proteins bind to the inner membrane face and coating of the external surface of the membrane by lipids of lamellar granules.
First, we want to know the average length of each cell. If you have 100 cells in a 1 millimeter space, we would do 1 ÷ 100. 1 ÷ 100 = 0.01 millimeters. Hope this helped!
Answer:
Option A.
The best way to carry out smart growth is by keeping neighborhoods walkable.
Explanation:
- Smart growth is an unique concept that avoids sprawl by urban framing plan and transportation theory.
- For the smart growth of the community there must be compulsorily availability of walkable spaces in a compact urban centers.
- This tool of smart growth helps in developing the cities by preserving the available spaces for tomorrow, this process is also known as the sustainable development.
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:
Unicellular. Bacteria are single-cell organisms. Bacteria are microscopic, usually 0.5 to 5 microns in length, and are generally smaller than eukaryotic cells. Unlike a human muscle cell or blood cell, a bacterial cell is a self-sufficient living being.
