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The simplest approach concatenates two (or more) interacting sequences and then employs the standard secondary structure folding algorithm with a slightly modified energy model that treats loops containing cut-points as external elements.
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Indirect interactions potentially emerge in any community of three or more interacting species [1], [2].
The observation that proteins with more interacting partners are subject to stronger levels of selective constraint suggests that direct protein protein interactions impose constraints on protein sequence evolution.
The more interacting with Duke, the more rewarding.
No more interacting.
We are given two potentially interacting sequences S and S of lengths n and m, respectively.
Nevertheless, the question of how to apportion causality between two or more interacting factors remains.
This implies that the chance of retrieving noise (false positive) remains low while predicting more interacting pairs.
To map with more detail the domain 1-interacting sequences we expressed different fragments of this domain (1a, 381 448; 1 154–154; and 1c, 1 380) and analyzed their capacity to incorporate into muNS inclusions.
However, refined mapping of Smad-interacting sequences have not been conducted.
Likewise, deletion of the Gα12-interacting sequence from the PC1 cytoplasmic domain abrogated its inhibition of Gα12-stimulated apoptosis.
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