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Experimentally exploring the conformational space sampled by domain reorientation in calmodulin.
The conformational space sampled by the two-domain protein calmodulin has been explored by an approach based on four sets of NMR observables obtained on Tb(3+)- and Tm( 3+)-substituted proteins, finding neither the extended helix conformation initially observed in the solid state for free calcium Calmodulin nor the closed conformation(s) adopted by calciumCalmodulin either alone or in its adduct with target peptide(s).
Paramagnetism-Based Restraints for Xplor-NIH
Modules that use paramagnetism-based NMR restraints have been developed and integrated in the well known program for solution structure determination Xplor-NIH and agreement between the two programs is quite satisfactory and validates both protocols.
Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains.
An innovative analytical/computational approach is presented to provide maximum allowed probabilities (MAPs) of conformations in protein domains not rigidly connected to calmodulin and to its adduct with alpha-synuclein.
Conformational space of flexible biological macromolecules from average data.
A rigorous method is developed to extensively sample the conformational space and to construct MO maps from experimental data, suggesting that Compact conformations in general have small MOs, whereas some extended conformations have MO as high as 35%, strongly suggesting these conformations to be most abundant in solution.
Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states
The homodimeric solution structures of S100A5 in both the apo and the calcium(II)-loaded forms have been obtained, and show a conformational rearrangement upon calcium binding, and a quite large mobility was observed in the hinge loop, which is not quenched in the calcium form.
Long-range correlated dynamics in intrinsically disordered proteins.
This study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems.