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BCL Conf is capable of reproducing bioactive conformations generating conformers that are structurally close to experimentally determined structures.
They exploit the vast amount of experimentally determined structures to derive statistical atom pair potentials.
FTIR and 500 MHz 1H NMR have determined structures and thermal stability was studied with DSC.
To study these interactions, we determined structures of "native" ribosome channel complexes derived from ER membranes.
Previously, we have determined structures of the hydrophilic domain in several redox states.
A comparison with previously determined structures identified a segment with remarkable conformational plasticity, induced by crystal contact effects.
Based on these newly determined structures, we propose a revised catalytic mechanism of peptide bond cleavage by DapE enzymes.
Previously determined structures along with this new structure provided a basis to test switch complex assembly models.
Some unknown protein structures are highly homologous to experimentally determined structures, such as Yes1 in the first case study.
In previous work, we determined structures of NPC1 NTD) in both cholesterol bound and free forms.
More experimentally determined structures or advances in structure prediction would be a necessary requirement for this to have broad applicability.
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