Nathan O. Kaplan – författare

Multiple Equilibria in Proteins covers the multiple interactions between small ions and molecules and a protein molecule. The book also deals with the physicochemical mechanisms of this interaction and the information about protein structure and the forces stabilizing that structure. The text discusses the mathematical description of complex formation, the thermodynamic analysis of binding data, and various theoretical models which can be used to describe the phenomena of small molecule-macromolecule interactions. The measurement of complex formation; the binding of neutral molecules; and hydrogen-ion equilibria are also considered. The book further tackles metal-ion binding; the binding of organic ions by proteins; as well as protein-protein interaction. Chemists and biochemists will find the book useful.

Molecular Photobiology: Inactivation and Recovery describes the deleterious photochemical reactions occurring in biological systems. This book is composed of 10 chapters that specifically tackle light interactions in the ultraviolet region of the spectrum resulting to damaged proteins and nucleic acids in living systems. This book deals first with the kinds of photochemical reactions that can occur and the possible effects of photochemistry on molecular, cellular, and organismal levels. The succeeding chapters highlight the principle of recovery mechanisms, wherein evidence shows that cells can repair their damaged genetic material, and thus recover from the otherwise inactivating effects of light. The remaining chapters are devoted to the comparison and contrast of some biological effects of ionizing radiation and those of ultraviolet radiation. This book is of value to molecular photobiologists, photochemists, biochemists, and radiation scientists and researchers.

Molecular Biology: An International Series of Monographs and Textbooks: Fluorescence Assay in Biology and Medicine, Volume II covers the many applications of fluorescence and phosphorescence. This book discusses the principles of fluorescence polarization, comparison of luminescence methods of analysis, and direct measurement of fluorescence decay times. The photodecomposition, sulfhydryl compounds, determination of primary structure, and fluorescent staining are also deliberated. This text likewise covers the assay of purines in nucleic acid hydrolyzates, formyltetrahydrofolate synthetase, and ovarian hormones. This volume is valuable to chemists, physicists, and biophysicists intending to use fluorescence in studying reaction mechanisms and elucidate the structure of complex biopolymers.

Protein Structure deals with the chemistry and physics of biologically important molecules—the proteins—particularly the determination of the structure of various proteins, their thermodynamics, their kinetics, and the mechanisms of different reactions of individual proteins. The book approaches the study of protein structure in two ways: firstly, by determining the general features of protein structure, the overall size, and shape of the molecule; and secondly, by investigating the molecule internally along with the various aspects of the internal configuration of protein molecules. It describes in detail experimental methods for determining protein structure in solution, such as the hydrodynamic method, the thermodynamic optical method, and the electrochemical method. The book then explains the results of experiments carried out on insulin, lysozyme, and ribonuclease. The text notes that the experiments, carried out on native and denatured proteins as well as on derivatives prepared by chemical modification (e.g., by methylation, iodination, acetylation, etc.), can lead to greater understanding of secondary and tertiary structures of proteins of known sequence. The book is suitable for biochemists, micro-biologists, cellular researchers, or investigators involved in protein structure and other biological sciences related to muscle physiologists, geneticists, enzymologists, or immunologists.