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This model implies that the ROS produced is not stoichiometrically linked to the number of disulfide bonds formed, but varies by the number of futile cycles before the correct bond is formed.
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Further, the correct bond valences require a knowledge of the relaxed structure which can be predicted from simulations.
The protein preparation steps included assigning correct bond orders, addition of hydrogens, creation of disulphide bonds, conversion of selenomethionine to methionine and capping of terminal residues.
Both RNAup and IntaRNA can not predict any correct bond for GcvB-gltI, since they missed the binding site.
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The result can be explained by the contrast in bonding strength between the correct and erroneous bonds.
She had symptoms for years before receiving the correct diagnosis.
Before the 1970s, bond investors paid for ratings directly.
Incoming ligands are 'caught' in site B before the actual bond formation process occurs.
Adjustments were made to the second and third layers to allow for the correct configuration for hydrogen bonding.
The correct placement of disulfide bonds is often rate-limiting in protein folding, notably of proteins which are secreted.
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