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Under kinetic control, the final protein aggregations are the outcome of maximizing the van der Waals interactions between side chains and backbone hydrogen bonds.
In the case of the β2-adrenoceptor (inactive: 2RH1, fully active: 3SN6), the distances in the inactive state are 3.9 Å between side chains and 10.0 Å between Cαs, whereas in the fully active state the distances are 3.9 and 9.3 Å, respectively.
Work to understand the electronic effects of the aromatic side chain substituents in these materials led to the subsequent discovery of aromatic interactions between side chains and main chains that control the conformations of solid-state phenylene-ethynylene oligomers, including highly twisted conjugated backbones.
The local structural environments of amino acids were first defined as suggested by Overington and colleagues [28], [29]: 1) main-chain conformation and secondary structure, 2) solvent accessibility and 3) hydrogen bonding between side chains and main chains.
While CAO was determined using coarse-grained Cβ side chain contacts, STRIKE uses a more sophisticated definition of contacts discriminating between side chains and backbone.
The binding of ligands to proteins often results in structural changes that promote interaction between side chains and the ligand in the binding site.
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A positive φ torsion angle can be accommodated by a Gly, which has no side chain, but for most other L-amino acids it leads to disallowed interactions between side-chain and main-chain atoms.
The hydrophobic residues, Phe and Trp, provide hydrophobic interactions between side-chains and intermolecular recognition by π−π interactions, Orn and Glu provide strong coulombic and complementary electrostatic interactions, and Gln, Orn and Glu side-chains make one surface of the β-sheet more hydrophilic than the other.
This distinction between side-chain and ring-modified oxysterols is in agreement with the observed functional differences between these oxysterol classes.
In each of the two dimers, the coiled-coils are stabilised by a pair of salt bridges between side chains of K160 and D161.
(A ) Structure of the unlocked state illustrating the hydrogen bond between side chains of N44 and E35 that stabilises this intermediate species.
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