The amino acids, as denoted by the name, contain amino and carboxyl groups. Each amino acid has the amine group connected to a central carbon, which is then connected to a carboxyl group.

Amino acids may contain R-groups on the central carbon, and all amino acids have a specific R-group except for glycine, which is the simplest amino acid. Glycine is bound to an extra hydrogen atom in place of an R-group. Only methionine can start a protein structure; methionine is coded by the start codon on an mRNA sequence. Some amino acids are capable of forming alpha-helices, while others are capable of disrupting and breaking alpha-helices. Proline, for example, frequently disrupts this secondary structure. Each protein is coded by a specific sequence of amino acids; not all proteins will contain every amino acid.

tRNA, or transfer RNA, is responsible for binding amino acids and delivering them to the ribosome during translation. tRNA binds amino acids with its anticodon. The anticodon is a sequence of 3 nucleotides that are complimentary to the codon of a specific amino acid. Anticodons can only bind to codons that are complementary in sequence; this ensures that the correct amino acids are chosen.

Cysteine is an amino acid that contain a sulfhydryl group . When two sulfhydryl groups come together and get oxidized they form a bond, which is referred to as a disulfide bond or a disulfide bridge.

Amino acids are the building blocks of proteins. The general structure of an amino acid consists of a carboxylic acid and an amine group bonded to a carbon that contains. The carbon contains an R group that varies depending on the amino acid.

The effects of point mutations vary by type. For example, leucine has 6 different codons. If the codon UUA is changed to UUG, the resulting amino acid inserted into the protein is not changed; it is still leucine. This is referred to as a silent mutation.

The effect of a point mutation is not dependent on the amino acid—the amino acid's selection is entirely independent of its structure. The amino acid selection during translation depends only on the three base-pair codon read by the ribosome. For example, the start codon—AUG—recruits methionine. If a frameshift mutation lead to UGG as the codon instead, tryptophan would be recruited. No single amino acid is more likely to be incorporated after a point mutation.

Proteins are polymers of amino acids, which have an amino group, carboxyl group, and a side chain known as an R-group. Nucleotides make up DNA and RNA. Glucose is a carbohydrate monomer and make up starches, cellulose, and glycogen. Fatty acids are components of lipids.

Peptide bonds are the uniquely named form of covalent bonds that hold together amino acids. These bonds are formed when the carboxylic acid of one amino acids reacts with the amino group of another amino acid. The result is a peptide polymer, known as a polypeptide, and a water molecule.

Glycosidic linkages are seen in sugars, and are used to bind monosaccharides. Hydrogen and ionic bonds are more general intermolecular forces. Hydrogen bonding helps shape the secondary and tertiary structure of proteins, but does not help in the formation of an amino acid chain.

A nitrogenous base is a part of the DNA/RNA structure. They include adenine, guanine, cytosine, thymine, and/or uracil. All other answer choices are parts of amino acids.

Amino acids are compounds that make up proteins and polypeptide chains. They are made up of an amine group , a carboxylic acid group , and a variable side chain. The amine group is called the “N terminus” and the carboxylic acid group is called the “C terminus”. The N terminus of one amino acid and the C terminus of another amino acid can form a peptide bond through a condensation reaction.