In biochemistry, the native state of a protein is its operative or functional form. All protein molecules are simple unbranched chains of amino acids, but it is by assuming a specific three-dimensional shape that they are able to perform their biological function. In fact, shape changes in proteins are the primary cause of several neurodegenerative diseases, including those caused by prions and amyloid. Biochemistry is the study of the chemical processes and transformations in living organisms. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Neurodegenerative disease (Greek νέυρο-, néuro-, nerval and Latin dÄ“generāre, to decline or to worsen) is a condition in which cells of the brain and spinal cord are lost. ... A prion (IPA: [1] ) — short for proteinaceous infectious particle (-on by analogy to virion) — is a type of infectious agent composed only of protein. ... Amyloids are insoluble fibrous protein aggregations sharing specific structural traits. ...

Many enzymes and other non-structural proteins have more than one native state, and they operate or undergo regulation by transitioning between these states. However, "native state" is used almost exclusively in the singular, typically to distinguish properly folded proteins from denatured or unfolded ones. In other contexts, the folded shape of a protein is most often referred to as its "conformation" or "structure." Ribbon diagram of the enzyme TIM, surrounded by the space-filling model of the protein. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Protein folding is the process by which a protein assumes its characteristic functional shape or tertiary structure, also known as the native state. ... Irreversible egg protein denaturation and loss of solubility, caused by the high temperature (while cooking it) In biochemistry, denaturation is a structural change in biomolecules such as nucleic acids and proteins, such that they are no longer in their native state, and their shape which allows for optimal activity. ... In chemistry, a chemical conformation is the spatial arrangement of atoms in a molecule. ...

Folded and unfolded proteins are often easily distinguished by virtue of their water solubilities, as many proteins become insoluble on denaturation. Proteins in the native state will have defined secondary structure, which can be detected spectroscopically, by circular dichroism and by nuclear magnetic resonance (NMR). A representation of the 3D structure of the Myoglobin protein. ... Circular dichroism (CD), is the differential absorption of left- and right-handed circularly polarized light. ... Pacific Northwest National Laboratorys high magnetic field (800 MHz) NMR spectrometer being loaded with a sample. ...

The native state of a protein can be distinguished from a molten globule, by among other things, distances measured by NMR. Amino acids widely separated in a protein's sequence may touch or lie very close to one another within a stably folded protein. In a molten globule, on the other hand, their time-averaged distances are liable to be greater. A molten globule (MG) is a stable, partially folded protein structure found in mildly denaturing conditions such as low pH (generally pH = 2), mild denaturant, or high temperature. ... A protein primary structure is a chain of amino acids. ...

Learning how native state proteins can be manufactured is important, as attempts to create proteins from scratch have resulted in molten globules and not true native state products. Therefore, an understanding of the native state is crucial in protein engineering. Protein engineering is the application of science, mathematics, and economics to the process of developing useful or valuable proteins. ...

External Links

• How to Run Native Protein Gels