Intrinsically disordered regions (IDRs) of proteins, when tethered to folded domains, function either as flexible tails or as linkers between domains. Most IDRs are composed of a mixture of oppositely charged residues. Recent measurements of tethered polyampholytes have shown that arginine- and lysine-rich sequences tend to behave very differently from one another.
Click here for original story, Research team untangles more secrets of intrinsically disordered regions of proteins
Source: Phys.org