Structural properties of trimers and tetramers of ribonuclease A

Protein Science : a Publication of the Protein Society
A NenciMassimo Libonati

Abstract

Ribonuclease A aggregates (dimers, trimers, tetramers, pentamers) can be obtained by lyophilization from 40% acetic acid solutions. Each aggregate forms two conformational isomers distinguishable by different basic net charge. The crystal structure of the two dimers has recently been determined; the structure of the higher oligomers is unknown. The results of the study of the two trimeric and tetrameric conformers can be summarized as follows: (1) RNase A trimers and tetramers form by a 3D domain-swapping mechanism. N-terminal and C-terminal types of domain swapping could coexist; (2) the secondary structures of the trimeric and tetrameric conformers do not show significant differences if compared with the secondary structure of monomeric RNase A or its two dimers; (3) a different exposure of tyrosine residues indicates that in the aggregates they have different microenvironments; (4) the two trimeric and tetrameric conformers show different susceptibility to digestion by subtilisin; (5) dimers, trimers, and tetramers of RNase A show unwinding activity on double-helical poly(dA-dT) x poly(dA-dT), that increases as a function of the size of the oligomers; (6) the less basic conformers are more stable than the more basic ones, an...Continue Reading

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Citations

Jan 16, 2002·Protein Science : a Publication of the Protein Society·Yanshun LiuDavid Eisenberg
Mar 7, 2009·Biochemical and Biophysical Research Communications·F Grant PearceJuliet A Gerrard
Feb 12, 2008·Biochimica Et Biophysica Acta·Giovanni Gotte, Massimo Libonati
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