Answer:
B: only amino acids join together with peptide bonds to form proteins.
Large polymers are created during dehydration synthesis, which are typically referred to as biological macromolecules. These compounds include proteins, lipids, carbohydrates, and nucleic acids.
As a result, the dehydration reaction is responsible for the formation of protein, lipid, and nucleic acids.
1. Protein structure
- Amino acid polymers form proteins. There are four different types of proteins, based on structure.
- The amino acid sequence of a protein is represented by its primary structure, which is a linear chain.
- The backbone (main chain) atoms of a polypeptide are arranged locally in space to form the protein's secondary structure.
- A polypeptide chain's whole three-dimensional structure is referred to as a protein's tertiary structure.
- The protein's quaternary structure, which is a three-dimensional arrangement of the subunits of a multi-subunit protein.
2. Lipid structure is a crucial element of the cell membrane. The structure is mostly composed of a glycerol backbone, two hydrophobic fatty acid tails, and a hydrophilic phosphate group.
3. Nucleic acids' structure: Nucleotide polymers make up nucleic acids. Each nucleotide is made up of an aromatic base with a N-atom connected to a pentose sugar with five carbons, which is then joined to a phosphate group.
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Answer:
https://guides.lib.purdue.edu/c.php?g=352816&p=2377942#:~:text=figures%20and%20tables.-,Discussion,the%20reasons%20for%20the%20errors.
Explanation:
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Answer:
Thalidomide may be defined as a type of the sedative drug that in the earlier time referred for the pregnant ladies. This drug causes the world wide tragedy and acts as a teratogen.
This drug causes mutation in the fetus. The Ames test is effective to understand the mutagenicity of the drug. In this test, if the auxotrophic strain of the bacteria is grown on the the deficient media containing thalidomide drug. The bacteria growth indicates the positive Ames test and the substance is considered as mutagen.
