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These observations may be related to the recognized role of CD4 in inducing conformational changes in gp120 that contribute to the exposure of binding sites for CXCR4 and CCR5 [ 16, 17, 38].
An aspect that has received considerably less attention is that the molecular packing arrangement of collagen and its microfibrillar arrangement at the fibril surface is a critical aspect governing the exposure of binding sites available to collagenolytic macromolecules.
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Because the induction of conformational changes in the integrin receptors 49 regulate the exposure of the binding site, the ligand-binding domain of the activated integrin heterodimer needs to be located at a defined minimum distance.
CD4 binding induces extensive structural rearrangements in gp120, resulting in the exposure of a binding surface for the second host cell chemokine receptor, CCR5 or CXCR4 [ 55, 56].
The increase is attributed to the exposure of latent binding sites after the pretreatment.
Considering the exposure of the binding site, there is no correlation between this property and any of the program performances.
The exposure of the binding site was calculated by using the SiteMap package [41] version 3.3 (Schrödinger).
The SiteMap package [27] version 3.3 (Schrödinger) was used to calculate the exposure of the binding site, which measures the degree of openness of the site to solvent.
We preferred the exposure of the binding site to the percentage SASA of the ligand, because the latter is based on the prior knowledge of the structure of the protein ligand complex, which is far from being the case when docking is needed.
Thin filament activation, which gives rise to isometric tension, is defined as the exposure of myosin binding sites [16] by the movement of Tm away from a position that blocks these sites on the actin filament.
Our method was more robust to the conformational changes, but more sensitive to the exposure of the binding ligands.
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