PubMed · 10421585
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P A Kollman. 1999-07-15. Hydrogen bonding.. https://doi.org/10.1016/s0960-9822(99)80319-4
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Structural and thermodynamic characterizations of a variety of intra- and intermolecular interactions stabilizing/destabilizing protein systems represent a major part of multidisciplinary efforts aimed at solving the problems of protein folding and binding. To this end, volumetric techniques have been successfully used to gain insights into protein hydration and intraglobular packing. Despite the fact that the use of volumetric measurements in protein-related studies dates back to the 1950s, such measurements still represent a relatively untapped yet potentially informative means for tackling the problems of protein folding and binding. This notion has been further emphasized by recent advances in the development of highly sensitive volumetric instrumentation that has led to intensifying volumetric investigations of protein systems. This paper reviews the volumetric properties of proteins and their low-molecular-weight analogs, in particular, discussing the recent progress in the use of volumetric data for studying conformational transitions of proteins as well as protein-ligand, protein-protein, and protein-nucleic acid interactions.
The relaxor based ferroelectric (1-x)Pb(Zn(1/3)Nb(2/3))O(3)-xPbTiO(3) and (1-x)Pb(Mg(1/3)Nb(2/3))O(3)-xPbTiO(3) single crystals provided new challenges in property characterization because their extraordinarily large piezoelectric coefficients and electromechanical coupling coefficients. Large errors may occur in some of the derived material constants using conventional characterization techniques. This paper will analyze the inadequacy of the traditional characterization methods and provide some basic guidelines for properly characterizing piezoelectric materials with extremely high piezoelectric and electromechanical coupling coefficients.
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