Biological macromolecules globular protein

There is considerable experimental evidence indicating loss of biological activity of macromolecules such as globular proteins and enzymes at gas-Hquid [57], liquid-solid (Fig. 26) [107] and liquid-liquid [108] interfaces. The extent of inactivation has been shown to be strongly influenced by the prevailing flow field and by, many other factors including the presence and/or absence of additives and contaminants and the type of solid surfaces (Figs. 27 and 28) [107]. 

Our discussion of globular protein structure begins with the principles gleaned from the earliest protein structures to be elucidated. This is followed by a detailed description of protein substructure and comparative categorization. Such discussions are possible only because of the vast amount of information available over the Internet from resources such as the Protein Data Bank (PDB www.rcsb.org/pdb), an archive of experimentally determined three-dimensional structures of biological macromolecules. 

This behavior can be seen as complementary to another aspect of protein folding the withdrawal of hydrophobic side chains from solvent. The latter minimizes perturbation by burying those portions of the polypeptide for which water is the poorest solvent. The former minimizes perturbation of solvent by what remains exposed. Not all biological macromolecules show so small an effect. Nucleic acids require for their hydration about twice the amount of water required by globular proteins (for heat capacity measurements comparing protein and tRNA, see Rupley and Siemankowski, 1986). It may be signihcant that DNA, with an extensive hydration shell, undergoes facile hydration-dependent conformational transitions, which are not found for proteins. 

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