Structural Properties of Staphylococcal Nuclease in Oligomeric A-Forms

V. N. Uversky^1,2* 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

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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.

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KEY WORDS: staphylococcal nuclease, partially-folded state, anion-induced forms, association

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