Structural properties of staphylococcal nuclease in oligomeric A-forms.
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.
Uversky
V N
VN
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia. uversky@vega.protres.ru
Fink
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AL
D000838:Anions; D019281:Dimerization; D008836:Micrococcal Nuclease / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
D000838:Anions; D008836:Micrococcal Nuclease