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- W2143893513 abstract "Domain swapping is a type of oligomerization in which monomeric proteins exchange a structural element, resulting in oligomers whose subunits recapitulate the native, monomeric fold. It has been implicated as a potential mechanism for protein aggregation, which provides a strong impetus to understand the structural determinants and folding mechanisms that trigger domain swapping. Bovine pancreatic ribonuclease A (RNase A) is a well-studied protein known to domain swap under extreme conditions, such as lyophilization from acetic acid. The major domain-swapped dimer form of RNase A exchanges a β-strand at its C-terminus to form a C-terminal domain-swapped dimer. To study the mechanism by which C-terminal swapping occurs, we used a variant of RNase A containing a P114G mutation that readily domain swaps under physiological conditions. Using NMR and hydrogen-deuterium exchange, we find that the P114G variant has decreased protection from hydrogen exchange compared to the wild-type protein near the C-terminal hinge region. Our results suggest that domain swapping occurs via a local high-energy fluctuation at the C-terminus." @default.
- W2143893513 created "2016-06-24" @default.
- W2143893513 creator A5043858304 @default.
- W2143893513 creator A5053849238 @default.
- W2143893513 date "2011-09-12" @default.
- W2143893513 modified "2023-10-14" @default.
- W2143893513 title "Propensity for C-terminal domain swapping correlates with increased regional flexibility in the C-terminus of RNase A" @default.
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- W2143893513 doi "https://doi.org/10.1002/pro.708" @default.
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