Fundamental chemical properties

Farrington, J. W. and Westall, J. (1986). Organic chemical pollutants in the oceans and groundwater a review of fundamental chemical properties and biogeochemistry. In The Role of the Oceans as a Waste Disposal Option, ed. Kullenberg, G., NATO ASI Series, D. Reidel, Boston, pp. 361 125. 

It was attempted to describe the fundamental chemical properties of flavins in some depth and to correlate them, whenever possible, to those of flavoproteins. It is obvious that, considering the wealth of information available, not all properties of flavin received the same attention which is reflected in the literature cited. 

Protein structure and function are the topics of this and the next three chapters. We begin with a description of the fundamental chemical properties of amino acids, peptides, and proteins. 

We now turn to polymers of amino acids, the peptides and proteins. Biologically occurring polypeptides range in size from small to very large, consisting of two or three to thousands of linked amino acid residues. Our focus is on the fundamental chemical properties of these polymers. 

Actinides, particularly the lighter ones, display multiple oxidation states and complex chemical behavior, which makes their chemistry quite fascinating. Some isotopes of these elements, such as 232Th, 233,235,238 and 239Pu, are important for the nuclear industry due to their utility as fissile/fertile materials. Therefore, the separation chemistry of different oxidation states of Th, U, and Pu need to be reviewed with respect to both basic as well as applied aspects. Some fundamental chemical properties of the lighter actinides, including oxidation states, hydrolysis, and complexation characteristics form the basis of their separation. 

Again, by definition, the negative logarithm to the base 10 of Ka, termed pKa, is usually reported. pKa is a fundamental chemical property and the subject of countless physical chemistry textbooks its theory will not be defined further here. In defining pKa we should also define pKb (the base dissociation constant) ... 

Two of the hydrophihcity scales in Table 2 were derived from experimental measures of the behavior of amino acids in various solvents, namely partitioning coefficients [K-D index of Kyte and Doolittle (30)] or mobility in paper chromatography [Rf index of Zimmerman et al. (31)]. By contrast, the Hp index was obtained from quantum mechanics (QM) calculations of electron densities of side chain atoms in comparison with water (32). The Hp index is correlated highly with these two established hydrophobicity scales (Table 4). Therefore, like the polarizability index, it is possible to represent fundamental chemical properties of amino acids (hydrophUicity, Hp) with parameters derived from ab initio calculations of electronic properties. However, in contrast to polarizabihty (steric effects), hydrophihcity shows significant correlation with preference for secondary structure. Thus, hydrophobic amino acids prefer fi-strands (and fi-sheet conformations) and typically are buried in protein structures, whereas hydrophilic residues are found commonly in turns (coil structure) at the protein surface. 

In this book we shall learn something of the fundamental chemical properties of the carbohydrates, knowledge that is basic to any further study of these compounds. 

Correlative methods are derived relationships between fundamental chemical properties of a substance and measured physical or chemical properties. They provide information about an oil from readily measured properties (ASTM D-2140,ASTM D-2501, ASTM D-2502, ASTM D-3238). 

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