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Description

Interaction of the bHLH-zip domain of c-Myc with H1-type peptides characterization of helicity in the H1 peptides by NMR

Journal of the European Academy of Dermatology and Venereology: JEADV

The highly conserved active site (CysGlyProCys), and the two cysteine residues at positions 32 and 35 are responsible for the disulphide reductase activity of Trx1 by reducing disulphide bonds on target proteins to form free thiol groups [11] (Figure 4)

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