Amino acids consist of an amine, a carboxylic acid, a hydrogen atom and a side chain (often simply referred to as an “R group”). Differences between these side chains are what differentiate amino acids from one another. These four components are bound to a central carbon atom, giving each amino acid a stereocenter. Amino acids form peptide bonds through condensation reactions between the carboxyl group of one residue and the amino group of another.

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.

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.

The number of codons can be found by raising the number of nitrogenous bases to the power of the codon length. In the genetic code, there are four bases and codons are three bases in length.

If codons were four bases in length, then the number of possible bases would be raised to the fourth power.

Every amino acid has a central carbon with an amino terminus and a carboxyl terminus. There is also a hydrogen attached to the central carbon. The last substituent varies between amino acids and determines how the particular amino acid will be used in proteins. This variable group is known as the "R-group." Only one amino acid, alanine, has a methyl group attached in the "R-group" position.

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.

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.

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.

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. 

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.