https://www.selleckchem.com/EGFR(HER).html
These interactions are significantly attenuated when N-IC is bound to NudE, suggesting that NudE binding shifts the conformational ensemble to one that is more extended and with less structure in H2. While the intrinsic disorder and flexibility in N-IC modulate its ability to serve as a binding platform for numerous partners, deviations of this protein from random-coil behavior provide a process for regulating these binding interactions and potentially the dynein motor.Na+/H+ antiporters comprise a super-family (CPA) of membrane proteins that
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