Explain the observations: 1. Two proteins have the same molecular weight and con

Question

Explain the observations:

1. Two proteins have the same molecular weight and consist of a single polypeptide chain w/240 hydrophilic amino acids and 60 hydrophobic a.acids, yet one is an integral protein and the other is a soluble protein.

2. In the legs of a reindeer, the membranes of cells near the hoofs have a higher portion of unsaturated fatty acids than the membranes of cells in the rest of the leg.

3. Most agents used in anesthetics are non-polar and act by increasing fluidity of the lipid bilayers of cellular membranes to the extent that the transmission of nerve impulses are disrupted and sensations of pain are eliminated.

Explanation / Answer

1. Two proteins with same molecular wieght and single polypeptide chain containing 240 hydrophilic amino acids and 60 hydrophobic acids, need not to be the same proteins. - There will be difference in the sequence alignment of the amino acids, and folding differs for both. - There are many hydrophillic and hydrophobic amino acids, and both proteins may have different amino acid composition. - In the case of soluble protein, the hydrophobic amino acids may fold inward, imparting solubility to the protein. -Integral protein have specific domains, that attach with the membranes. 2. It is because the temperature of body tissues at the hooves, generally will be low than center of the body. To maintain fluidity, membranes at lower temperatures must contain higher percentage of unsaturated fatty acids. A percent of unsaturated fatty acids will lower the melting point of lipid mixtures. 3. Anesthetics are non-polar and act by increasing fluidity of the lipid bilayers of cellular membranes. Due to this the permeability of cellular membrane will increase and the anesthetics will bindto the sodium channels, there by preventing the nerve transmission.

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