The number of possible tetrapeptides that can be made using all 20 amino acids i

Question

The number of possible tetrapeptides that can be made using all 20 amino acids is a. 20^4 b. 4^20 c. 4 times 20 d. 4 times 3 times 2 times 1. The number of subunits (poly peptide chains) and their entanglements provide which structures of proteins a. Primary b. Secondary c. Tertiary d. quaternary Human and bovine (beef hemoglobin differ from each other a. only in their secondary structures b. only in their tertiary structures c. only in their quaternary structures d. in their primary structures Hydrogen bonding between the backbones of protein chains can be found in a. the alpha helix b. the beta-pleated sheet c. both of these The quaternary structure of a protein describes a. The spatial relationship of subunits within the protein b. The number of s-s bridges c. The non-helical portions of globular proteins d. The number of hydrophobic interactions between the non-adjacent parts of the same polypeptide chain Detergents such as sodium dodecyl sulfate ca

Explanation / Answer

7.For 4 positions, each of which could be any 1 of 20 possibilities, there are 20 * 20 * 20 * 20 = 160,000 unique tetrapeptides.Hence the answer is option A

For 8,10,11,

The primary structure of a protein is its sequence of amino acids.

Most proteins have segments of their polypeptide chains repeatedly coiled or folded in patterns that contribute to the protein’s overall shape. These coils and folds, collectively referred to as secondary structure, are the result of hydrogen bonds between the repeating constituents of the polypeptide backbone (not the amino acid side chains).

While secondary structure involves interactions between backbone constituents, tertiary structure is the overall shape of a polypeptide resulting from interactions between the side chains (R groups) of the various amino acids. One type of secondary structure is the helix, a delicate coil held together by hydrogen bonding between every fourth amino acid while another one is the pleated sheet.

Finally, Some proteins consist of two or more polypeptide chains aggregated into one functional macromolecule. Quaternary structure is the overall protein structure that results from the aggregation of these polypeptide subunits.

Hence the answers are 8-d,10-c,11-d

9.Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron- and oxygen-binding protein in blood.

Myoglobin is oxygen carrier in muscles. It has nearly 17000 Dalton of molecular mass. It is a single polypeptide chain. It has only one Heme group. So it can bind reversibly to only one Oxygen molecule.

Whereas, Hemoglobin is oxygen transporter in Blood. It is present in RBC. It has 4 Heme Group. Hence it can bind to 4 Oxygen molecules. Hemoglobin has a Quaternary Structure characteristic of many multi-subunit globular proteins. Its Molecular mass is 64000 Dalton.1 Dalton(Da)= 1.660539040(20)×1027 Kg

Hence the answer is c

12.Detergent has a hydrophobic side and a hydrophilic side (When it dissolves grease, it forms protective bubbles from the water by surrounding grease molecules with the hydrophobic side). Proteins have hydrophobic and hydrophylic sides, the deregent is attracted to these and forces the protein apart. A protein's 3-D structure is partially created by hydrophobic and hydrophylic interactions to itself, the detergent substitutes this self bonding with detergent-amino acid bonding.

The answer is A

13.proteins are made up of peptide bonds and they are chemically called polyamides since they have NH bonds

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