1. Apoprotein: This is the protein portion, which is a polypeptide chain with a specific amino acid sequence.

2. Non-protein component: This is the non-protein part, which can be a variety of molecules, including:

* Prosthetic groups: These are organic molecules that are tightly bound to the apoprotein, often covalently. Examples include heme in hemoglobin, retinal in rhodopsin, and flavin adenine dinucleotide (FAD) in many enzymes.

* Coenzymes: These are organic molecules that are loosely bound to the apoprotein and can dissociate easily. Examples include NAD+, NADP+, and coenzyme A.

* Metal ions: These can be bound to the apoprotein through various interactions. Examples include iron in ferritin, zinc in carbonic anhydrase, and magnesium in chlorophyll.

Therefore, conjugated proteins are essentially protein-non-protein complexes. The non-protein component is often essential for the function of the protein, contributing to its activity, stability, or structure.

Here are some examples of conjugated proteins:

* Hemoglobin: A protein involved in oxygen transport. It consists of four globin protein chains, each bound to a heme prosthetic group.

* Lipoproteins: These proteins transport lipids in the bloodstream. They are composed of apoproteins and lipids, such as cholesterol and triglycerides.

* Glycoproteins: These proteins have carbohydrates attached to them. They are found in cell membranes, blood, and other tissues, and play diverse roles in cell signaling and recognition.

The specific combination of apoprotein and non-protein component determines the function and properties of a particular conjugated protein.