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Again, the variants mapping to the β-sheet domain and its subsequent loop disclosed the most pronounced alterations consistent with severe conformational changes.
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To simulate realistic conformational changes, several approaches have been proposed.
In Y133H, the induced conformational changes led to a severe destabilization and almost complete loss-of-function with a residual catalytic activity of 3.5%.
Under conditions of severe stress or apoptosis, translation of HEL67 could be diminished and/or conformational changes within the ribosome could alter HEL67-rRNA interactions, hence allowing RNases to attack the non-translating ribosomes and to initiate rRNA breakdown.
Structural comparisons suggest no global conformational changes upon putrescine binding to AdoMetDC; however, several local conformational changes are observed.
Conformational changes were monitored by Raman spectroscopy.
The conformational changes after adsorption are studied.
Protein molecules often undergo conformational changes.
Both homodimers and heterodimers undergo conformational changes upon activation.
Necessarily, the proteasome undergoes large conformational changes during its operation.
This neglects the conformational changes induced by ligand.
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