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In the Snf7 protofilament, the protomer (i) interacts with the next protomer (i+1) through both hydrophobic and electrostatic interactions, burying ~1060 Å of solvent-accessible surface area per protomer.
With this, the repulsion is modeled by (3) ψ (x 1, …, x M ) = ∏ i = 1 M exp (min j : j < i D (Θ i, Θ j ) ). Replica i interacts with its nearest neighbor j *, such that j * = arg min j : j < i D (Θ i, Θ j ).
Next, we determined whether the tumor suppressor p27 serves as a potential target for UCA1 because a previous report suggested that hnRNP I interacts with p27 and enhances p27 translation through interaction with the IRES, leading to cell cycle arrest.
The model could well explain the structural basis for the observed dimerization of 60S subunits by Sdo1p: domain I interacts with the ribosomal P-site of one subunit, while domains II-III (mostly II) interact with H38 of the other subunit.
It is not clear what proteins cucurbitacin I interacts with to prevent actin depolymerization.
Residue Glu37R in switch I interacts with the invariant Arg388G on helix α9.
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For drug d i interacting with T i targets, t p i and t q i ~ denote the target interacting and not interacting with d i, respectively.
During these studies, we preliminary found that TFII-I interacted with the BRCT domain.
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