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Авторизация |
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Поиск по указателям |
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Branden C., Tooze J. — Introduction to protein structure |
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Предметный указатель |
Isotypes 300
Jacob, Francois 143
James, Michael 210
Jansonius, Hans 52
Janus protein 369T 370
Jelinski, Lynn 290
Jelly roll barrel in two sheets 78
Jelly roll barrel, canonical 335 336F
Jelly roll barrel, formation 77—78
Jelly roll barrel, viruses 335 335F
Jelly roll barrel, VP1 of rhinovirus 337 338F
Jelly roll domain, SV40 and polyomavirus VP1 342
Jelly roll motif 77
Jelly roll motif, formation/folding 77—78 77F
Jelly roll motif, hemagglutinin 80 81F
Jelly roll structure, picornaviruses 335 336F
Jelly roll structure, spherical plant viruses 335—337 335F 336F
Johnson, Louise 106
Jones, Alwyn 69
Jun 191 192 199
jun gene 199
Jun, amino acid sequence 192F
Junction diversity, immunoglobulins 302
Jurnak, Frances 255
Kallikrein 362
Kaptein, Robert 164 181
Karle, Jerome 379
Kendrew, John 13 13F 14 370F 379—381 380F
Kent, Stephen 9
Keratins 287
Kim, Peter 96
Kim, Sung-Ho 106 255
Kinderstrom-Lang, Kai 28
Kinemage Supplement 23
Kinetic factors, protein folding 91—92
Klevit, Rachel 177
Klug, Aaron 176 181 183 327 330
Koshland, Daniel 113
Kossiakoff, Anthony 267
Kraut, Joseph 215
Kretsinger, Robert 24 25
Kringle domains 29F
Kuhlbrandt, Werner 241
Kunitz domains 361 361F
Kunitz domains, inhibitors 361
Kunitz domains, phage-optimized sequences 362T
Kuriyan, John 273 276
Kyte, J. 245
L amino acids 5 9
L subunit, photosynthetic reaction center 235 236—237 246F
L subunit, photosynthetic reaction center, conservation between species 246—247
L subunit, photosynthetic reaction center, pigments bound to 237—239
L-form of amino acids 5 9
Lac operon 143 146
Lac repressor 143—145
Lac repressor, binding to major and minor DNA grooves 143—145 145F
Lac repressor, helix-turn-helix motif 144 145F
Lac repressor, subunit structure 144 144F
Lac repressor, V-shape tetrameric structure 144 145F
LACI-D1 (Lipoprotein-associated coagulation inhibitor D1) 361 362 362T
Lactate dehydrogenase, Rossman fold 47
Ladner, Robert 362
Lambda bacteriophage see “Bacteriophage lambda”
Laue diffraction picture 374F 376
Lazarus, Robert 362
Lens, crystallin structure 74 74F
Lesk, Arthur 22F 23 42 311
Leucine zippers 175 191—193 202
Leucine zippers in b/HLH/zip family 196F 199—200
Leucine zippers, definition 192
Leucine zippers, dimerization interactions 191—193
Leucine zippers, globular proteins using coiled coils 287
Leucine zippers, heterodimers 192—193 193F
Leucine zippers, side chain interactions 192 193F
Leucine, structure 6F
Leucine, x-ray diffraction data 382
Leucine-rich motifs 47 55 56F
Leucine-rich motifs, -horseshoe fold 55—56
Levinthal, Cyrus 91
Lewis, Mitchell 143
LH1 and LH2 see “Light-harvesting complexes”
Ligand-binding sites, helix 16
Ligand-binding sites, orientation importance 270 (see also “Receptors”)
Light chains see under “Immunoglobulin(s)”
Light-harvesting complexes 240—241
Light-harvesting complexes, LH1 241
Light-harvesting complexes, LH1, antenna protein ring 242—244 243F
Light-harvesting complexes, LH2 241
Light-harvesting complexes, LH2, circular ring of chlorophyll 241 241F 242F 243
Liljas, Lars 339 340
Linker regions, -zinc cluster family binding to DNA 190—191 190F
Linker regions, GAL4 binding to DNA 189
Linker regions, growth hormone binding to prolactin receptor 270 270F
Linker regions, transducin 256
Lipid-binding proteins 70
Lipids, membrane 223 246—247 253
Lipscomb, William 60
Loop regions 21—22
Loop regions in barrels 49
Loop regions in motif 28
Loop regions, b/HLH family 200
Loop regions, b/HLH/zip family 200
Loop regions, carboxypeptidase 61 61F
Loop regions, CDK2(T-loop) 108
Loop regions, chymotrypsin 211 211F 212
Loop regions, complementarity determining regions 311
Loop regions, GroES 102
Loop regions, growth hormone receptor 267 267F
Loop regions, hairpin 21—22 21F
Loop regions, homeodomains 160
Loop regions, immunoglobulins 304—305 304F 305—306
Loop regions, model building from x-ray diffraction data 383
Loop regions, movements time scale 105
Loop regions, MyoD 197
Loop regions, neuraminidase 71 71F
Loop regions, omega loop 22
Loop regions, p53 169—170 171 171F
Loop regions, prediction 21
Loop regions, Ras protein 255—256
Loop regions, serpins 111
Loop regions, spherical viruses 335—336
Loop regions, three-dimensional structure 21
Loop regions, variable in homologous proteins 349—350
Loop regions, “open” and “closed” conformations 22
Low, Barbara 27
Lysine, GAM binding to DNA 188 189F
Lysine, recognition helix of glucocorticoid receptor 184—185
Lysine, specificity of serine proteinases 213
Lysine, structure 6F
Lysine, trypsin mutation 215
Lysozyme, antilysozyme complex, structure 310—311 310F
Lysozyme, Fab binding 309—310 310F
Lysozyme, folding pathways 95—96 95F
Lysozyme, structure 310—311
Lysozyme, T4 bacteriophage see “Bacteriophage T4”
Lytic-lysogenic cycle switch 130—131 130F 133
M subunit, photosynthetic reaction center 235 236—237 246F
M subunit, photosynthetic reaction center, conservation between species 246—247
M subunit, photosynthetic reaction center, pigments bound to 237—239
MacKinnon, Roderick 232 234
Magnesium, activation 258
Magnesium, GTP linking to Ras protein by 255 255F
Magnesium, LH2 light-harvesting complex 241
Main-chain, formation 4 4F
Main-chain, modeling of protein structures 349
Main-chain, polarity 14
Major histocompatibility complex 300 (see also “MHC molecules”)
Malaria, resistance and sickle-cell hemoglobin 43—45 44F
Maltoporin 230
Mandelate racemase 54—55 54F
| Mandelate, conversion to benzoate 54—55 54F
Mariuzza, Roy 317
Mat 162
Mat gene, homeodomain 162 162F
Mat repressor 160
Mat -Mat al complex 163 163F
Matthews, Brian 132 134 354 355
MAX 175 192F
Max, binding to DNA 200F
Max, heterodimer with Myc 199
Max, homodimers 199—200
Max, monomer structure 200F
Max, sequence-specific interactions with DNA 201 201F
Mayo, Stephen 367
Mcm1 162
McPherson, Alexander 312
Melting temperature (Tm) 354 356F
Membrane fusogen, hemagglutinin as 80
Membrane lipids 223 246—247 253
Membrane proteins 223—250
Membrane proteins, crystallization, difficulties 224
Membrane proteins, crystallization, novel methods 224—225
Membrane proteins, functions 224
Membrane proteins, signal transduction 251
Membrane proteins, solubilization by detergents 224 225F
Membrane proteins, two-dimensional crystals and EM 225—226 226F
Membrane proteins, types 223 223F
Membrane-bound proteins, helices 35
Membranes 223
Membranes, functions 224
Mengo virus 333 336
Menten, Maud 206
Met repressor 175
Metal atoms, in proteins 11 11F
Metallo proteinases 205
Metallo proteins 11
Methallothionein, NMR and x-ray, crystallography comparison 391
Methionine, structure 7F
Methylmalonyl-coenzyme A mutase, , barrel domain 50—51 50T
MHC genes 314—315
MHC genes, polymorphism 315
MHC molecules 300 312—313
MHC molecules, antigen recognition 314—315 316
MHC molecules, Class I 300
MHC molecules, class I, antigen-binding site 314
MHC molecules, class I, peptide binding 315F 316
MHC molecules, class I, peptide complexes 318 318F
MHC molecules, class I, structure 312 313 313F
MHC molecules, Class II 300
MHC molecules, class II, domains 315
MHC molecules, class II, peptide binding 315—316 315F
MHC molecules, domains 313—314 313F
MHC molecules, peptide complex as ligand for T-cell receptor 318 318F
MHC molecules, structures 312—313
MHC molecules, synthesis 316
Michaelis — Menten equation 206F
Michaelis — Menten scheme 206 206F
Michaelis, Leonor 206
Michel, Hartmut 234 241
microtubules 284
Milligan, Ronald 295
Mineralocorticoid receptor 181F
Model building, antigen-binding sites of immunoglobulins 349—350
Model building, Cro-DNA interactions 134—135
Model building, hypervariable regions, immunoglobulins 349
Model building, x-ray diffraction data 381—382 382F
Modeling of protein structures 349
Molecular chaperones see “Chaperones”
Molecular disease see “Sickle-cell anemia”
Molecular dynamics simulations 105
Molten globular proteins 89 92 92F
Molten globular proteins, barnase folding intermediate 94
Monoclonal antibodies, CDR conformation prediction 350 350F
Monod, Jacques 113 117 142 143
Monomeric proteins 29
Motifs 13—34 29
Motifs in barrel and sheet structures 47—48 49F
Motifs, motif see “ motif”
Motifs, combined into domains 29 30
Motifs, Greek key see “Greek key motif”
Motifs, hairpin see “Hairpin motif”
Motifs, jelly roll see “Jelly roll motifs”
Motifs, simple 24—26
Motifs, simple, combination into complex motifs 30—31 (see also “ helices” “ “Loop “Other
Muconate lactonizing enzyme 54 54F
Muirhead, Hilary 51
Multimeric proteins 29
Multiple isomorphous replacement (MIR) 379—380
Multiwavelength Anomalous Diffraction (MAD) 381
Muramidase, bacterial 39 39F
Muscle contraction 292
Muscle contraction, ATP role 296—297
Muscle fibers 290—291
Muscle fibers, thick and thin filaments 290 291 “Myosin”)
Mutagenesis, oligonucleotide-directed 359F
Mutagenesis, random 359 359F
Mutagenesis, site-directed 163—164
Mutations, DNA shuffling method 365—366
Mutations, enzyme evolution 55
Mutations, point 366
Mutations, protein folding studies 93—95
Myc 191
myc gene 199
Myc, heterodimer with Max 199
Myeloma proteins 309
MyoD 197
MyoD, helix region 197 198—199
MyoD, binding to DNA 198F
MyoD, dimerization region structure 197F
MyoDsequence-specific interactions with DNA 201
Myofibrils 291F
Myogenic proteins 197
Myoglobin as domain structure 35
Myoglobin, breathing of molecule 105
Myoglobin, globin fold in 40
Myoglobin, oxygen binding 105
Myoglobin, structural irregularity 13
Myoglobin, structure 384
Myoglobin, structure, computer-generated schematic diagram 22F
Myoglobin, structure, early results 13 13F
Myoglobin, structure, schematic diagram 23F
Myoglobin, structure, two-dimensional 22F
Myoglobin, x-ray diffraction 379
Myohemerythrin 37 381F
myosin 36 197 256 290—291 291F
Myosin, actin complex, structure 295 295F
Myosin, conformational change 294—295 296
Myosin, cross-bridge movement 291—292 295
Myosin, cross-bridge movement, confirmation 292—293 295—296
Myosin, nucleotide-binding cleft 295 296
Myosin, S1 fragment 294 294F 295
Myosin, sliding filament model 291 291F
Myosin, structure 292 294—295 294F
Myosin, swinging cross-bridge hypothesis 292 292F 295—296 296F
Nef protein 275 275F 276F
Neuraminidase 70—71
Neuraminidase, active site 71F 72
Neuraminidase, amino acids 71
Neuraminidase, folding motifs in propeller-like structure 71—72 71F 73F
Neuraminidase, function 70—71
Neuraminidase, subunit structure 71 71F 72F
Neurofilament proteins 287F
Neurospora crassa, PRA isomerase and IGP synthase 53
Neutrofil elastase 110
NF-kB 168—169
NMR 374 387—388
NMR, advantages 391
NMR, COSY 388 388F 389
NMR, distance constraints 390—391
NMR, folded protein flexibility 105
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