作者: E.R. Simons , E.R. Blout
DOI: 10.1016/S0021-9258(18)99347-6
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摘要: Abstract The circular dichroism of ribonuclease A, S, S-protein, S-peptide, and S' has been measured in aqueous solutions the 215 to 300 mµ region. spectra A S are virtually identical; that is similar but lacks a positive peak at 240 mµ. S-protein exhibits more negative ellipticity between 232 265 Upon addition S-peptide this region becomes less negative. These differences tentatively attributed changes contribution tyrosyl residue near Ribonuclease exhibit no maximum below pH 2 3.5, respectively; dependence suggests side chain carboxylic acid interaction occurs.