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Mutagenesis studies in Rb. capsulatus C cP have shown that the interface at which the enzyme interacts with its electron donor cyt c2 involves nonspecific salt bridge interactions, as the extent of the interaction is dependent on the ionic strength of the solution.
Hydrogen bonds and salt bridge interactions are delineated by black dashed lines.
L-arginine binds tightly to the enzyme via a network of hydrogen bonds and salt bridge interactions.
This discrepancy highlights the difficulty of modeling salt bridge interactions with a protein design algorithm that approximates side chains as discrete rotamers.
Exhaustive analysis of the simulated Boceprevir-bound wild and mutant complexes revealed variations in hydrophobic interactions, hydrogen bond occupancy and salt bridge interactions.
Site-directed mutagenesis and molecular dynamics simulations have revealed that the inactive state conformations are stabilized by specific interhelical and intrahelical salt bridge interactions and hydrophobic-type interactions.
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By contrast, comparable stopped-flow circular dichroism studies indicate that the salt-bridge interactions, with one possible exception, are not well formed in the transition state for folding.
Further, coiled-coil formation is disrupted by protonation below pH 6.0, with a corresponding decrease in Trp fluorescence emission intensity, demonstrating that salt-bridge interactions play a critical role in maintaining the structural integrity of the apoE CT domain.
These salt-bridge interactions play important roles in the initial compaction of the molecule.
(C ) Table of hydrogen bond and salt-bridge interactions in the Norrin dimer interface.
Via interaction with troponin-C, CaT enables cross-bridge interactions for myocardial force generation/shortening.
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