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Structural Properties of Staphylococcal Nuclease in Oligomeric A-Forms

V. N. Uversky1,2* and A. L. Fink3

1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia; fax: (095) 924-0493; E-mail: uversky@vega.protres.ru

2Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia

3Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA

* To whom correspondence should be addressed.

Received August 25, 1997
Association affects the structural properties of different partially folded conformations of staphylococcal nuclease induced by anions of different nature. It is shown that oligomerization induces new structural levels in non-native A-forms. A close structural similarity between the monomeric A2 and the dimeric (A1)2 forms as well as between the monomeric A3 and oligomeric [(A1)2]M and [A2]M forms is established. This suggests that association of a protein molecule in partially folded conformations can be an additional structure forming factor.
KEY WORDS: staphylococcal nuclease, partially-folded state, anion-induced forms, association