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Protein denaturation is the process in which a protein loses its native structure and function due to external factors like temperature, pH, or chemical agents. This causes the protein to unfold and lose its specific three-dimensional structure, rendering it unable to perform its biological activity. Three examples of protein denaturation are: 1. Heat-induced denaturation: High temperatures can cause proteins to lose their structure, as seen when cooking an egg, where the proteins in the egg white and yolk denature, leading to solidification and change in texture. 2. pH-induced denaturation: Changes in pH can cause proteins to lose their structure, like in the curdling of milk, where casein proteins denature due to decreased pH as lactic acid forms. 3. Chemical-induced denaturation: Specific chemicals can disrupt non-covalent interactions within proteins, like when ethanol disrupts hydrophobic interactions in alcohol-based hand sanitizers, leading to the denaturation and inactivation of proteins in pathogens.