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Introduction
In his Nobel Prize–winning hypothesis, the biochemist Christian Anfinsen postulated that the native, biologically active conformation of a polypeptide chain represents a kinetically accessible unique free energy minimum (Anfinsen 1973). Its simplified form, “one sequence–one structure,” has played an extremely useful role, helping make sense of the structural principles of protein function; but there is growing evidence that it is not always true. Three-dimensional (3D) domain swapping is a phenomenon that violates the dogma in a particularly elegant way. It is quite ironic that the flagship of 3D domain swapping is ribonuclease A (RNase A), the very protein used by Anfinsen to work out his dogma. 3D domain swapping is a mechanism of protein oligomerization, in which a structural element of a protein fold is replaced by an identical element from another subunit. Some proteins, for instance, RNase A, can assume many...
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Jaskolski, M. (2013). 3D Domain Swapping. In: Roberts, G.C.K. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16712-6_431
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DOI: https://doi.org/10.1007/978-3-642-16712-6_431
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