Abstract
The side-chain potential surfaces of Glu 35 and Asp 52 residues of the lysozyme active center were investigated on the basis of a semiempirical method of conformational analysis. It has been shown that small changes of about ± 20° around the global minima are possible for the dihedral angles of these two catalytic residues.
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Schedule a callMore From: ARI - An International Journal for Physical and Engineering Sciences
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