Increase of RNase A N-terminus polarity or C-terminus apolarity changes the two domains' propensity to swap and form the two dimeric conformers of the protein

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From: Biochemistry(Vol. 45, Issue 36)
Publisher: American Chemical Society
Document Type: Article
Length: 65 words

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Abstract :

The influence of the hydrophilic or hydrophobic character of the N- and C-terminal ends of RNase A on the oligomerization of ribonuclease A by 3D domain swapping is explored. The results provide strong evidence t that protein oligomerization in general and RNase A oligomerization in particular, occurring through the 3D domain-swapping mechanism, could be influenced by the hydrophilic or hydrophobic character of their swapping domains.

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Gale Document Number: GALE|A153217502