Protein mutations may lead to pathologies by causing protein misfunction or propensity to degradation. For this reason, several studies have been performed over the years to determine the capability of proteins to retain their native conformation under stress condition as well as factors to explain protein stabilization and the mechanisms behind unfolding. In this review, the author explores the paradigmatic example of frataxin, an iron binding protein involved in Fe-S cluster biogenesis, and whose impairment causes Friedreich's Ataxia (FRDA). The review summarizes what is known about most common point mutations identified so far in heterozygous FRDA patients, their effects on frataxin structure and function and the consequences of its binding with partners.

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