By Mukesh Doble
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Extra resources for Biotransformation and Bioprocesses (BIOTECHNOLOGY AND BIOPROCESSING SERIES)
Coming to the catalytic activity, the active site or the center must be of a deﬁned or highly ordered geometry if it is to contain all the binding and catalytic groups in correct alignment for optimal catalysis. This imposes a heavy entropy demand on the system. This can be compensated at the expense of another already ordered region of the biopolymer losing its organization, as the enzyme binds to a substrate. For that matter, it is these two functions, namely the molecular recognition and catalytic activity, that necessitate the macromolecule to be highly ordered and organized.
The lowest energy conformer is the state in which any molecule will exist in ground state. Thus, for cyclic structures, such as cyclopentane and cyclohexane (which we normally encounter in biologic systems), the probable low-energy conformers are the envelope form for the cyclopentane and the two chair forms for the cyclohexane (as shown in Fig. 11). One has to be cautious when applying these above principles because based on the substitutions on theses ring systems the lowest energy conformer may be diﬀerent.
Side chains that are uncharged will tend to have low solubility in water–nonpolar amino acids. At the opposite end of the polarity scale are the charged side chains, which have high solubility in water–polar amino acids. Histidine has ambiguous polarity, in a sense it has a dual character due to imidazole ring. 2 General structure of alpha-amino acid. Copyright 2004 by Marcel Dekker, Inc. All Rights Reserved. 3 Structures of amino acids. Copyright 2004 by Marcel Dekker, Inc. All Rights Reserved.
Biotransformation and Bioprocesses (BIOTECHNOLOGY AND BIOPROCESSING SERIES) by Mukesh Doble