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Protein folding is a very sensitive process that is influenced by several external factors including electric and magnetic fields, temperature, pH, chemicals, space limitation and molecular crowding. These factors influence the ability of proteins to fold into their correct functional forms.
Protein folding is crucial for normal physiology including development and healthy aging, and failure of this process is related to the pathology of diseases including neurodegeneration and cancer.
Protein misfolding is a common cellular event that can occur throughout the lifetime of a cell, caused by different events including genetic mutations, translational errors, abnormal protein modifications, thermal or oxidative stress, and incomplete complex formations.
The protein folding problem is the question of how a proteins amino acid sequence dictates its three-dimensional atomic structure. The notion of a folding problem first emerged around 1960, with the appearance of the first atomic-resolution protein structures.
Folding of proteins into their correct native structure is key to their function. Failure to fold properly produces inactive or toxic proteins that malfunction and cause a number of diseases.
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Answer and Explanation: Enzymes have a tertiary protein structure which is maintained by interaction between amino acid R groups. This complex folding is responsible for creating the specific shape of the enzymes active site, through which it attaches to a specific substrate.
The sequence of amino acids that make up the protein chain determines its folding pattern. Protein folding is important because it determines how the protein interacts with other molecules, how it moves and changes shape, and ultimately, its function.

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