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Knowing the native state topology in examining proteins is important because it allows researchers to get an accurate view of a protein’s processes, reactions, and binding affinities. This process also helps researchers keep proteins stable.
However, some researchers do not understand why it is important to measure under native conditions, opting for easier circumstances. Here’s why measuring under native conditions is important for multiple laboratory processes, from protein unfolding to affinity measurement and more.
What Does “Native Conditions” Mean?
When you measure something under native conditions, such as a protein, you look at how the protein assembles or folds itself in its proper form. Simply put, you look at how the protein looks as it occurs in nature. This condition is the operative and functional form of the protein, allowing researchers to see how the protein will react to certain chemicals and reactions naturally. Measuring under an unfolded state will not provide this same information.
Chains of amino acids make up the basic structure of all proteins. However, these chains fold onto themselves to make very specific three-dimensional shapes that vary by the type of protein, known as the tertiary structure. All of these folded structures have free energy and allow the protein to perform its biological function.
Sometimes, proteins can unfold in a process known as denaturation. This process takes the protein out of its native state and native conditions. While the protein may produce some biological reactions, denatured proteins are not a good indication of how the substance will act in natural reactions.
The Importance of Measuring Under Native Conditions
When scientists measure under native conditions, they are receiving the best possible look at how a protein interacts in nature. These observations provide the basis for several scientific studies across the biological disciplines. If a researcher examined what a protein’s interactions were like in a non-native state, the results may not be as accurate.
Measuring under native conditions is vital for the development of remedies to several diseases and medical conditions. For example, shape changes in proteins lead to the development of many diseases, including neurodegenerative diseases such as mad cow disease or kuru. Researchers use measurements under native state conditions to help develop remedies for these diseases and restore people’s health.
Researchers can learn how to manufacture native condition proteins to use them in experiments. Some researchers may even attempt to create the protein from scratch – previous attempts to do so, without understanding the native conditions, have led to the development of unstructured globules instead of the protein. By understanding how the protein folds onto itself in nature, scientists can use this data in replication and the construction of new technologies, especially in the medical and pharmaceutical fields.
What Happens If You Don’t Measure Under Native Conditions?
If a protein unfolds or a scientist cannot measure the protein in its native state, they cannot look at how the protein operates in its functional, biological form. Unless the researcher needs to look at a certain disease that an unfolded protein causes, not measuring under native conditions could pose issues for the research. Researchers who need to look at proteins in their natural, functional state will need to establish native conditions in their experiments.
When you are conducting an experiment in your lab, always make sure to measure under native conditions as often as possible. You’ll receive better, more accurate results to benefit your research. Unless you want to look at denaturation, a protein that unfolds itself and develops a disease, or any other protein abnormality, rely on native conditions to successfully complete your experiment.