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The influence of side chain architecture is then considered.
Our results show a correlation between the increase of side chain motion amplitude and catalytic efficiency.
IR spectra indicated involvement of side chain unsaturation in bond formation leading to cross-linking.
Our procedure also allows for the optimization of side chain torsion angles of protein residues within the binding pocket.
The role of side chain interactions in the formation of AG BDA complexes in aqueous solutions was confirmed by NMR.
By designing constitutionally isomeric perylene monoimide (PMI) amphiphiles, we studied the effect of side chain sterics on nanostructure crystallization.
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Addition of side chain-cleaving enzymes to the core enzymes increased depolymerization of a more complex model substrate, oat spelt xylan.
Hydrolysis of side-chain amide groups to acid groups was observed during the thermal aqueous degradation.
We compare our results with the observed distributions of side-chain dihedral angles in proteins of known structure.
Through careful adjustment of side-chain DP, carbons with surface area as high as 420 m2/g were obtained.
Packed helices move relative to each other, these shifts being accommodated by motions of side-chain atoms arising from small changes in torsion angles.
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