During heparin-induced self-aggregation of the four repeat domain peptides (R1–R4) excised from tau, R1, which resembles Tau Peptide (244-274), was the most resistive to filament formation. Its conformation remained unchanged. The peptide maintained the same random structure under both acidic and neutral conditions.
During heparin-induced self-aggregation of the four repeat domain peptides (R1–R4) excised from tau, R1, which resembles Tau Peptide (244-274), was the most resistive to filament formation. Its conformation remained unchanged. The peptide maintained the same random structure under both acidic and neutral conditions.
| Pack size available | 0.5mg, 1mg |
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