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Upon docking of the agonist to its receptor, this H-bond is broken and the molecule adopts a more extended structure.
The apoA-I molecule adopts a two-domain tertiary structure and the properties of these domains modulate the ability to form HDL particles.
Both compounds consist of two folded aromatic amide moieties, which are connected with an acetylene linker in 1 or directly in 2. The rigid conformations of their folded moieties are stabilized by intramolecular tri-centered hydrogen bonding, while the whole molecule adopts a 'S'- or 'C'-styled conformation depending on the relative orientation of the two rigid moieties.
The molecule adopts a β-sandwich fold with seven strands connected by six loops, similar to an immunoglobulin domain but without any disulfide bonds.
As the polyethylene oxide chain length increases, the molecule adopts a random coil conformation which may lead to a structured region around the non-polar part of the reactant.
Thus, the initial 'banana' shaped molecule adopts a (slightly) more evenly curved conformation when docked to the fibril surface.
Similar(48)
Ring-puckering analysis indicates that the molecule adopts an ideal chair conformation [51].
In the structures of Y122F and molecule A of other threes (WT1, F86YF87Y and WT-HP), the ADO molecule adopts an all-helical folding, comprising of eight α-helices (H1 H8) that form a compact structure (Fig. 1A and 1B).
For example, if a small molecule adopts an appropriate 3-D shape and possesses compatible functional groups properly oriented in 3-D space, it will likely bind to the biological moiety of interest.
The issue related to why this molecule adopted a left or right handed helical wind and what the factors influencing this balance might have been.
Substitution of chrysene in this manner resulted in the molecule adopting a twisted geometry; 12 has a torsional bend of 7.24° about the central bond of the molecule.
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