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Proteins are complex molecules, both structurally and functionally, and observing and monitoring their properties
can provide strong insights into how they work. One of the measurable properties of a protein is its stability, which
can be defined by the probability that it will unfold, or denature. But a protein is composed of a string of amino
acids, each with their own electrochemical properties, which means any change in temperature or electrochemical
balance in the protein's environment can upset its stasis, resulting in a destabilization event. For instance,
changes in pH, buffer composition, and charged molecules in the protein's environment can alter how well the
amino acids within the molecule can bind to each other. This can cause the protein to change its conformation, or
shape, or unfold and refold in a way that alters its properties. Proteins are most stable in their native folded state.
Subsequently, misfolded proteins can clump together, or aggregate, a phenomenon that has been linked to the
onset of many diseases.
What is
protein stability?
Derivative of image by Vincent Voelz - sent to the uploader personally, CC BY-SA 3.0,
https://commons.wikimedia.org/w/index.php?curid=21891212
