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1. The method of spin labeling 1 1.1. Introduction 1 1.2. Structure of nitroxide labels and probes 3 1.3. ESR signals of NRs: magnetic parameters 6 1.4. Methods of measurement of the ESR signal parameters 10 1.4.1. Stationary methods 10 1.4.2. Pulse methods 17 1.5. Rotational diffusion of nitroxides 21 1.5.1. General 21 1.5.2. Elements of the theory of the ESR spectra of rotating nitroxides 22 1.5.3. Very slow rotation 24 1.5.4. Slow-motion regions 29 1.5.5. Fast-rotation regions 31 1.5.6. Rotations in different regions 34 1.5.7. High-frequncy low-amplitude dynamics 36 1.5.8. Superslow motion 37 1.6. Nitroxides as dielectric, pH, and redox probes 38 1.7. Nitroxides in ESR tomography 41 1.8. Spin traps 43 2. Double-labeling techniques 46 2.1. General 46 2.2. Effects of spin-spin interactions on the parameters of ESR spectra 48 2.2.1. Principal effects 48 2.2.2. On the parameters of ESR signals of paramagnetics 50 2.2.3. Spin-spin interactions in biradicals and polyradicals and paramagnetic complexes of metals with nitroxide ligands 53 2.3. Determination of the distance between spins 57 2.4. The spin label-spin probe method 62 2.4.1. General 62 2.4.2. Selection of spin probes 66 2.4.3. Investigation of steric, electrostatic, and exchange effects 67 2.4.4. Determination of the immersion depth of a radical center 70 2.4.5. NRs in oxymetry 71 2.5. Nuclear magnetic resonance of paramagnetic systems 74 3. Fluorescent labeling methods 80 3.1. General 80 3.1.1. Absorption spectra 80 3.1.2. Fluorescence and phosphorescence 83 3.2. Chemical properties of fluorescent labels and probes 85 3.3. Rotational diffusion of fluorescent chromophores 93 3.3.1. Depolarization of fluorescence 93 3.4. Fluorescence and molecular dynamics of the medium 96 3.5. Study of local acidity and electrostatic and polar properties of biological objects 99 3.5.1. Measurement of pH 99 3.5.2. Measurements of electric charge density, transmembrane potential, and ion concentration 100 3.5.3. Measurement of polarity: on the dynamic polarity scale 102 3.6. Inductive resonance energy transfer as a method of investigating structures and dynamics of biological objects 104 3.6.1. Mechanism of inductive resonance energy transfer 104 3.6.2. Estimation of the distance between donor and acceptor groups 106 3.6.3. Orientation factor 107 3.7. Dynamic quenching of fluorescence as an approach to the study of molecular dynamics 111 3.8. Charge transfer complexes, excimers, and exciplexes as luminescent probes 112 3.9. Study of slow translational diffusion: photobleaching and fluctuation techniques 114 4. Triplet labeling methods 116 4.1. Peculiarities of triplet excited states 116 4.2. Structures and chemical properties of triplet probes 118 4.3. Exchange interactions with participation of excited triplet states: elements of theory 120 4.4. Static exchange: experimental data 124 4.5. Dynamic exchange processes 126 4.5.1. Elements of theory 126 4.5.2. Experimental data 127 4.6. Photochrome probes 130 4.7. The triplet probe-photochrome labeling method 133 5. M8ssbauer spectroscopy, electron scattering, and other labeling methods 136 5.1. M6ssbauer labels 136 5.1.1. Physical principles 136 5.1.2. Dynamic effects in M6ssbauer spectroscopy 139 5.2. NMR probes 141 5.3. Total tritium labeling technique 143 5.4. Electron-scattering labels 144 5.4.1. General 144 5.4.2. Physical grounds 146 5.4.3. Modification of biological objects by electron- scattering labels 148 5.4.4. Electron microscopy determination of shape and size of electron-scattering particles 154 6. Studies of proteins and enzymes: structure, dynamics, and mechanism of action 158 6.1. Active centers of enzymes 158 6.1.1. Serine proteases 158 6.1.2. Nitrogenase 161 6.1.3. Dehydrogenases 166 6.1.4. Cytochrome P-450 168 6.1.5. Myosin and actin 170 6.1.6. Other enzymes and proteins 171 6.2. Conformational changes in proteins and enzymes 175 6.2.1. Large-scale and allosteric conformational changes 175 6.2.2. Transglobular conformational transition 177 6.3. Molecular dynamic properties of proteins and enzymes 180 6.3.1. General 180 6.3.2. Experimental data 182 6.3.3. Dynamics and functional activities of proteins 188 6.4. Physical labeling as a tool for studying the electron transfer mechanism 195 6.4.1. General 195 6.4.2. Delocalization of spin density and local polarity in proteins 196 6.4.3. Collisions between molecules: steric factor 197 6.4.4. Mechanisms of dynamic adaptation at electron transfer 198 7. Structure and dynamics of membranes 201 7.1. Model membranes 203 7.1.1. Structure of model membranes: localization of labels and probes 203 7.1.2. Molecular dynamic properties and conformational transitions in model membranes 209 7.1.3. Mixed and protein-lipid model membranes 217 7.2. Biological membranes 221 7.2.1. Erythrocyte membranes 221 7.2.2. Sarcoplasmic reticulum 223 7.2.3. Rhodopsin membranes 225 7.2.4. Microsomes 226 7.2.5. Acetylcholine receptor 228 7.2.6. Membranes of chromatophores of photosynthetic bacteria 229 7.2.7. Other membranes 231 8. Nucleic acids and other biological systems: biological assays 233 8.1. Nucleic acids 233 8.1.1. Modification of nucleic acids with physical labels 233 8.1.2. Investigation of microstructure and conformational changes in nucleic acids 236 8.2. Polysaccharides 239 8.2.1. Glycoproteins 240 8.2.2. Cotton fibers and cellulose 241 8.3. Spin-labeled, physiologically active compounds 243 8.4. Cells, tissues, organisms 248 8.4.1. Distribution of labels: microcomponent localization of cells 248 8.4.2. Redox properties of cells 250 8.5. Biological assays 252 8.6. Biological analyses 255 8.6.1. Biologically active ions and compounds 255 8.6.2. Immunological assays 259