Exact(4)
Intrinsically disordered proteins (IDPs) are characterized by highly flexible solvent exposed backbones and can sample many different conformations.
Moreover, one end of the acceptor is buried in the active site cavity while the other end of the acceptor is exposed in the flexible solvent region.
The HADDOCK docking protocol consisted in three steps: randomization of orientations and rigid body minimization, semi-flexible simulated annealing in torsion angle space and flexible solvent refinement where the structures obtained after the semi-flexible simulated annealing are refined in an explicit solvent layer.
The flexible solvent exposed loop, which is not resolved in the X-ray structure connects the last α-helical region of the catalytic core to the first β-strand of the β-barrel 1 domain.
Similar(56)
This model was consistent with experimental NMR and SAXS data and displayed some unique features such as a Pro/Ala-rich non-polar insert, which formed a flexible solvent-exposed loop on the surface of the protein opposite to the IGF-binding interface.
Based on our experience with holo-AMPK, we introduced entropy-reducing mutations into flexible, solvent-exposed surface residues of AMPK α1 (11-353).
Unlike DNA polymerases from the five other families, the Y-family DNA polymerases have flexible, solvent-accessible active sites that are able to tolerate various types of damaged template bases and allow for efficient lesion bypass.
We could overcome the recalcitrance of holo-AMPK to crystallization in the absence of pharmacological activators by extensive construct screening and by altering three flexible solvent-exposed side chains (E471G/E474A/K476A) at the N-terminus of the ST-loop of the α-subunit (see Materials and Methods and Figure 2A).
In previous studies, we have identified by 1H Nuclear Magnetic Resonance (NMR) spectroscopy that Hsp25 and α-crystallin have short, flexible and solvent exposed C-terminal extensions, which protrude from the domain core of the molecule [16], [17], [18].
Chemical mapping with 1-methyl-7-nitroisatoic anhydride (1M7) in 100 mM NaCl and 6 mM MgCl2 (pH 8.0) to identify conformationally flexible and solvent accessible ribose rings gave results consistent with the crystal structure (29).
Our data indicated that cross-linking occurred across two identical conserved histidine residues on two separate heavy chains in the hinge region, which is highly flexible and solvent accessible.
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