Abstract
Abstract The reaction of potassium nitrosyldisulphonate (NDS) with globular proteins has been monitored by electron spin resonance. The reaction is shown to be sufficiently sensitive and reproducible to provide a rapid new method for the estimation of exposed tyrosine and tryptophan residues in these proteins at physiological pH. Under these conditions each tyrosine residue was found to consume 2 moles, and each tryptophan residue 3 moles, of NDS. The estimation of accessible groups thus obtained are in good agreement with published data obtained using other chemical probes.
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