Hydrolysis reactions involve breakdown of molecules (lysis) in the presence of water. Water is a reactant in hydrolysis reactions. Dehydration synthesis reactions involve formation of bonds between molecules (synthesis) and removal of water at the end of the reaction (dehydration). Water is a product in dehydration synthesis reactions.

During the formation of peptide bonds a hydroxyl group from carboxylic acid and a hydrogen atom from the amino group are released and form water. Formation of peptide bonds is a dehydration synthesis reaction because bonds are synthesized and water is released.

Formation and destruction of bonds within macromolecules always involve a hydrolysis or a dehydration synthesis reaction. Esterification and hydrogenation reaction refer to other organic chemistry processes.

Proteins are made up of amino acids that undergo a series of dehydration reactions, which link them together to form the primary structure of a protein. Amino acids are linked together by peptide bonds, while nucleic acids are linked via phosphodiester bonds. The secondary structure of the protein is formed by hydrogen bonding between the amino acid backbones. Every protein will have primary and secondary structure, and thus will have hydrogen bonding.

Disulfide bridges help to construct tertiary structure, but only occur between cysteine residues. Cysteine will not necessarily be present in every protein, and there are some proteins that cannot form disulfide bridges. Similarly, not all proteins will contain glycine.

Aldehyde groups are frequently found in carbohydrates, but do not often appear in proteins.

Whenever you think about disulfide bonds you should think about cysteine. Cysteine contains a sulfur atom in a sulfhydryl group that is capable of forming a disulfide bridge with another sulfur atom in another cysteine residue. These disulfide bridges contribute to the overall three-dimensional structure of the protein, namely the tertiary structure).

Quaternary structure results from the joining of multiple polypeptide subunits and is driven by hydrophobic interactions. Tertiary structure is also driven by hydrophobic interactions, but also relies on intermolecular forces between amino acid function groups, such as the cysteine sulfhydryl.

To block a receptor protein, a molecule must structurally resemble the natural ligand. The active sites of proteins are highly specific, and will only bind certain molecules. The chemical formula, electrons, and bonding in the molecule can all influence small regions of the molecule's structure, but the overall shape must ultimately match the active site of the target protein.

Though proteins may be found on the cellular membrane, they are not a primary component. The cell membrane is known as the "phospholipid bilayer," as it is primarily composed of a double layer of lipids. Proteins may be attached to the surface or fully integrated into the bilayer, and serve as a means of signaling, transport, and adhesion.

Proteins are a primary component of the endocrine system, and several signaling hormones are made of peptides. The proteins action and myosin are directly involved in muscle contraction and for the structural basis of the sarcomere. Enzymes are a special class of catalytic proteins. Chaperone proteins and ion channels help transport molecules through the body; many nonpolar molecules must bind to a protein to travel through the blood.

An enzyme lowers the energy of the transition state, which makes the chemical reaction proceed faster. Enzymes speed up many chemical reactions in processes like DNA synthesis and glycolysis. They are also proteins, so they're composed of amino acids.

Polypeptides are are polymers of amino acids. Proteins consist of one or more polypeptide chains folded in a certain shape. Polysaccharides are polymers of monosaccharides and do not contain amino acids. Cellulose is a polysaccharide that is a major component of plant cell walls.

The amino acid sequence is the primary structure of a protein, which is held together by peptide bonds. The secondary structure involves hydrogen bonding between the backbones of amino acids. Tertiary structure describes the unique folding pattern of a polypeptide as a result of intermolecular forces such as hydrogen bonds, hydrophobic interactions and covalent bonds such as disulfide bridges. Tertiary structure is the result of the amino acid side chains interacting with each other. Quaternary structure is the interaction of two or more polypeptide chains with each other.

Steroids fall into the lipid category, characterized by a carbon skeleton composed of four fused rings  Cholesterol is a type of steroid; it is synthesized in the liver, and is necessary for the production of sex hormones. Triacylglycerol is also a type of lipid, composed of three fatty acid molecules and a glycerol (also known as a triglyceride). Starch is a polymer of glucose monomers. Its primary function is to store energy. A protein is a molecule that is composed of polypeptides, folded into a 3D structure. Each protein is composed of a combination of amino acids. Proteins make up over 50% of dry mass of a cell and have many different functions like speeding up chemical reactions, defense, storage, transport, cellular communication, movement, and structural support. Enzymes are types of proteins that speed up chemical reactions, and are never consumed during reactions.

All of the protein structures will be altered and disrupted. Drug X disrupts the amino acid sequences in the primary structure of the protein. The primary structure acts as the protein’s blueprint. It can be concluded that if the primary sequence is altered, all of the subsequent structures will be disrupted as well. The sequence of amino acids encode for the protein’s particular shape and function; disrupting the code will change the shape and function of the primary, secondary, tertiary, and quaternary structures of the protein.