NATIVE AND FUSION PROTEINS OVERVIEW

The terms “native proteins” and “fusion proteins” are often used in the field of molecular biology to describe different types of proteins. Understanding the differences between these two types of proteins is crucial in various biological applications such as protein purification, functional studies, and drug development.

1) Native Proteins

Native proteins are naturally occurring proteins that exist in their functional and native form within the cell or organism. These proteins have a specific three-dimensional structure and function that is essential for their biological activity. Native proteins are typically isolated and purified from their natural sources, which can be cells, tissues, or organisms.

The process of isolating and purifying native proteins involves several steps, including extraction, solubilization, purification, and concentration. The goal is to obtain a pure preparation of the protein with minimal contamination from other cellular components. Native proteins are essential for various applications, such as structural studies, enzyme assays, and therapeutic development.

2) Fusion Proteins

Fusion proteins, on the other hand, are artificially created proteins that consist of two or more distinct protein domains joined together by a peptide linker. These proteins are designed to have specific properties or functions that are not present in the individual protein domains. Fusion proteins are commonly used in research, diagnostics, and therapeutics.

The process of creating fusion proteins involves the genetic manipulation of an organism’s DNA to insert the coding sequences for the desired protein domains. The fusion protein is then expressed in a host organism, such as bacteria or yeast, and purified for use in various applications. Some common uses of fusion proteins include:

1. Purification tags: Fusion proteins can be engineered to contain specific tags that facilitate protein purification. For example, a polyhistidine (His) tag can be added to the protein, which allows for the selective binding and purification of the fusion protein using metal affinity chromatography.
2. Protein-protein interactions: Fusion proteins can be designed to study protein-protein interactions by fusing two or more protein domains that interact with each other. This can help elucidate the molecular mechanisms underlying specific biological processes.
3. Therapeutic agents: Fusion proteins can be engineered to have enhanced biological activity or specificity compared to their native counterparts. For example, fusion proteins can be designed to target specific cancer cells or viruses, making them potential therapeutic agents.