This book is devoted to the physical and mathematical modeling of the formation of complexes of protein molecules. The models developed show remarkable sensitivity to the amino acid sequences of proteins, which facilitates experimental studies and allows one to reduce the associated costs by reducing the number of measurements required according to the developed criteria. These models make it possible to reach a conclusion about the interactions between different amino acid chains and to identify more stable sites on proteins. The models also take the phosphorylation of amino acid residues into account.
At the end of the book, the authors present possible directions of application of their physical and mathematical models in clinical medicine.
1. Introduction
2. Physical methods for studying proteins
Describe the various experimental approaches for determine the structure of molecules, the relative location of domains in space, the identification of active protein centers. Their advantages and disadvantages are shown:
2. Physical methods of protein studies
2.1. Electrophoresis method.
2.2. Chromatographic method
2.3. Spectral method.
2.4. X-ray analysis of protein crystals
2.5. Spectroscopy in the ultraviolet and visible range.
2.6. Spectrofluorimetric method
2.7. Circular dichroism.
2.8. Conclusions
3 Physical properties of amino acids and proteins.
tions
3.1. Structural organization of proteins.
3.2. The solubility of proteins.
3.3. Conclusions
4. Selection of a biological objects.
Presents the rationale for choosing a biologil#£