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Many proteins do not function as monomers in the cell, but interact with partners in stable or transient complexes.
However, many proteins do not link to others, indicating that their functions are unrelated or unknown.
Many proteins do require conserved amino acid sequences for ligand binding.
Many proteins do not act as monomers in the cell but as part of multimeric protein complexes that may include proteins encoded by one or several distinct genes.
These complications make it no surprise that many proteins do not achieve their correct conformations, or stably assume the wrong ones.
First, many proteins do not interact, while others may connect to major hubs that interact with hundreds of genes and proteins.
Similar(52)
Although in some cases partially cleaved products from proteolysis provide information on the structure of this elusive form, proteolysis of many proteins does not accumulate detectable intermediates.
Research of a past decade and a half leaves no doubt that complete understanding of protein functionality requires close consideration of the fact that many functional proteins do not have well-folded structures.
Soluble Slit2 did not have this effect, suggesting that the effect requires local, high concentration as many synaptogenic proteins do (Dean et al., 2003; Yumoto et al., 2012).
The actual genes destined for the extracellular and plasma membrane may vary as many membrane proteins do not have N-terminal signal peptides as they use internal signals to integrate into the ER membrane [ 19] and some of the proteins without signal peptides potentially use unconventional secretory pathways [ 20].
Many of these proteins do not appear to interact directly with the protostome TACCs, but would be expected to be in the same protein complex (Fig. 6C,6D).
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