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Since many proteins containing intrinsically disordered regions have similar abnormal migration on SDS-PAGE gels, we hypothesized that Atg31 may have characteristics of an intrinsically disordered protein (IDP).
Many proteins containing GGDEF or EAL domains are linked to various N-terminal sensory input domains, suggesting that several signals from the environment are integrated through the c-di-GMP signaling pathway.
Thus, while many proteins containing intramolecular disulphide bonds migrate more rapidly under non-reducing conditions due to the more compact native structure [40], p38 migrated faster in reduced than in oxidized state, a phenomenon suggesting that the more slowly migrating form could be engaged in intermolecular disulphide bonds [41] [43].
Many proteins containing zinc-finger structures have been demonstrated to be involved in oncogenesis.
Many proteins containing the chitin_bind_4 domain have been isolated from the cuticle of both insects and crustaceans.
Such regulation is documented and there are many proteins containing both a receiver domain and a DGC/PDE domain (PleD for example).
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However, many proteins contain independently folded subdomains that subsequently assemble into a supertertiary structure1.
Many proteins contain intrinsically disordered regions that are highly solvent-exposed and susceptible to post-translational modifications.
Notably, many proteins contain multiple copies of the UIM motif connected by linkers with different lengths.
Because many proteins contain multiple domains, many of these methods of protein clustering result in the establishment of incorrect families.
Many proteins contain Ser/Thr-Pro sequences; however, most of them are not phosphorylated by ERK, suggesting that there is a strict relationship in ERK substrate specificity [28].
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