Branden C., Tooze J. — Introduction to protein structure :: Электронная библиотека попечительского совета мехмата МГУ

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Branden C., Tooze J. — Introduction to protein structure

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Название: Introduction to protein structure

Авторы: Branden C., Tooze J.

Аннотация:

Introduction to Protein Structure gives an up-to-date account of the principles of protein structure, with examples of key proteins in their biological context generously illustrated in full colour to illuminate the structural principles described in the text. The first few chapters introduces the general principles of protein structure both for novices and for non-specialists needing a primer. Subsequent chapters use specific examples of proteins to show how they fulfil a wide variety of biological functions. The book ends with chapters on the experimental approach to determining and predicting protein structure, as well as engineering new proteins to modify their functions.

Язык:

Рубрика: Биология/

Статус предметного указателя: Готов указатель с номерами страниц

ed2k: ed2k stats

Издание: 2nd edition

Год издания: 1999

Добавлена в каталог: 29.03.2006

Операции: Положить на полку | Скопировать ссылку для форума | Скопировать ID

Предметный указатель

Domain-domain associations, immunoglobulin hypervariable region      307
domains      3F 29 29F
Domains from structural motifs      30
Domains, CDK2      107—108 107F
Domains, definition      29
Domains, GroEL      see “GroEL”
Domains, interdomain movements      109—110
Domains, large polypeptide chains      29—30
Domains, lysozyme      95F
Domains, movements      89
Domains, thioredoxin      97
Domains, types      29F (see also “ $\alpha$ domains” “ “ “
Doolittle, D.F.      245
Drenth, Jan      215
Drosophila      159 160 162F 179
Drug design, for common cold      337—338 337F
DsbA      96 97 97F
DsbA as oxidizing agent      98
Dystrophin      36
Edmundson, Allen      304
EF motif (EF hand)      24 25F
EF motif (EF hand), amino acid sequences      26F
EF motif (EF hand), calmodulin      110
Eisenberg, David      353
Elastase      212—213 213F
Electron microscopy      374
Electron microscopy, membrane proteins      225—226 226F
Electron microscopy, myosin cross-bridges      292
Electron microscopy, transthyretin      288
Electron-density map      381—382 382F 384
Electron-transfer reactions      11
Electronic area detectors      377
Electrons, scattering      378
Electrons, transfer in photosynthesis      239
Electrons, x-ray interactions      381
Elongation factor, Tu      255
Emphysema      113
Endoplasmic reticulum, MHC molecule loading      316
Energy, folded and denatured state of proteins      90
Energy, light, conversion to electrical energy      239—240
Engelman, D.A.      245
Engrailed gene      160 162F
Engrailed homeodomain      162F 165
Enhancer elements, distal      151 151F 152
Enhancer elements, distal, distance from promoters      152
Enhancer elements, GAL4 zinc cluster, regions binding to      188—189 189F
Enteroviruses      333
Enthalpy, folded/denatured proteins      90
Entropy, cost of folding proteins      354
Entropy, native/denatured state of proteins      90
Enzyme(s), and $K_{cat}$ values      206
Enzyme(s), $\alpha/\beta$ barrels      48—49
Enzyme(s), activation energy of reactions decreased by      206—207 207F
Enzyme(s), antibodies as      see “Antibodies catalytic”
Enzyme(s), catalysis      see “Catalysis”
Enzyme(s), catalytic properties      206
Enzyme(s), evolution      54—55
Enzyme(s), in protein folding      89
Enzyme(s), multidomain subunits      51
Enzyme(s), R and T states      114—117
Enzyme(s), R and T states, phosphofructokinase      115 116—117 117F
Enzyme(s), reactions      see “Catalysis”
Enzyme(s), transition-state affinities      207 207F
Enzyme-linked receptors      251
Enzyme-linked receptors, classes      270—271
Enzyme-linked receptors, tyrosine kinase receptors      270—271
Enzyme-substrate (ES) complex      206
Epidermal growth factor (EGF)      29F
Epinephrine      253 254
Erabutoxin      26 26F
Erythropoietin      364
Erythropoietin receptor (EPOR), agonists, phage display of random peptide libraries      364—365
Erythropoietin receptor (EPOR), EMP1 peptide      364 365 365F
Erythropoietin receptor (EPOR), extracellular domain (EBP)      364 365 365F
Escherichia coli, arabinose-binding protein      62—63 62F
Escherichia coli, bacteriophage growth      129—130
Escherichia coli, DsbA structure      97 97F
Escherichia coli, heat-shock proteins      see “GroEL” “GroES”
Escherichia coli, lac operon      143—145
Escherichia coli, maltoporin      230
Escherichia coli, met repressor      175
Escherichia coli, phosphofructokinase      115—116 115F
Escherichia coli, porins      229
Escherichia coli, PRA isomerase and IGP synthase      53 53F
Escherichia coli, ribonucleotide reductase      11 11F
Estrogen receptor      181 181F 183
ethane      10F
Eucaryotic cells, disulfide bridge formation      96
Evans, Phil      50 115
Evolution, $\gamma$ -crystallin      76
Evolution, antibodies, T-cell receptor and MHC      300
Evolution, chymotrypsin      210 212
Evolution, combinatorial methods accelerating      358—359
Evolution, conservation of $\alpha$ domains      41—42
Evolution, conservation of heme pocket      43
Evolution, directed, recombination and mutation in      365—366 366F
Evolution, DNA shuffling      365—366
Evolution, enzymes      54—55
Evolution, globin fold preservation      41—42
Evolution, homeodomain proteins role      159—160
Evolution, immunoglobulin domains      301
Evolution, jelly roll barrel structures of viruses      335—337 335F
Evolution, new enzyme activities and $\alpha/\beta$ barrels      54—55
Evolution, POU-specific domains      166
Evolution, proteinases      205
Evolution, serine proteinases      210
Evolution, subtilisin      210
Evolution, transcription factors      202
Evolutionary relatedness, primary structure of proteins      29
F-actin      293
Fab fragments      303 304 306 307F 308F
Fab fragments, lysozyme complex      309—310 310F
Factor IX      29F
Familial amyloidotic polyneuropathy      288
Fatty acids, synthesis      30
Fc fragment      303 312
Fe atom, in photosynthetic reaction center      236 238
Feedback inhibition      113
Feedback, negative loop      142
Feher, G.      246F
Fersht, Alan      60 93 357
Fiber diffraction methods      384—385 385F
Fiber diffraction methods, biopolymers      386—387
Fiber diffraction methods, diffraction patterns      385F
Fiber diffraction methods, diffraction patterns, DNA      386—387 386F
Fiber diffraction methods, diffraction patterns, transthyretin      288
Fibers, symmetry      384
Fibers, x-ray diffraction      see “Fiber diffraction methods”
Fibrils      283 285
Fibrinogen, heptad repeats      36
Fibronectin type III domain      267 319 319F
Fibrous proteins      283—298
Fibrous proteins, amyloid and transthyretin      288—289
Fibrous proteins, coiled-coil $\alpha$ helix      35
Fibrous proteins, oligomers, coiled coil $\alpha$ helices      286—287
Fibrous proteins, silk fibroins      289—290 (see also “Actin” “Collagen” “Myosin”)
Filamentous bacteriophage      359—361 360F
Filaments      283
Flavodoxin      24F 58F 59
Fletterick, Robert      213
Flexibility of proteins      91
Flexibility of proteins, folded proteins      104—105
FMN-binding redox protein      58F 59
Fold recognition (threading)      353—354
Folding of proteins      see “Protein folding”
Foot-and-mouth disease virus      333
Fos      191 192 199
fos gene      199
Fos, amino acid sequence      192 192F
Fos-Jun heterodimer      192—193

Four-helix bundle      37—39 38F
Fourier transform      379
Fourier, Jean Baptiste Joseph      379
Franklin, Rosalind      121 387
Free energy      90 92 93
Freeman, Hans      24F
Frog muscle      292—293
Fructose—6-phosphate (F6P)      114F 115 116 117
FSD-1 peptide      368 368F 368T
Functions of proteins      3
Fusogen, hemagglutinin as      80
fyn      274 275
G protein-linked receptors      251
G proteins      252—264
G proteins as GTPases      252 259—260
G proteins as molecular amplifiers      252—254
G proteins, $G_{\alpha}$       252
G proteins, $G_{\alpha}$ , $G_{\beta\gamma}$ binding blocked by phosducin      265—266
G proteins, $G_{\alpha}$ , activation by switch region change      257—259
G proteins, $G_{\alpha}$ , GTP complex structure      256
G proteins, $G_{\alpha}$ , GTP hydrolysis mechanism      260 260F 261F
G proteins, $G_{\alpha}$ , GTPase domain binding to $G_{\beta}$       263—264
G proteins, $G_{\alpha}$ , inactive and active forms      258F
G proteins, $G_{\alpha}$ , Ras comparison      256—257
G proteins, $G_{\alpha}$ , RGS regulating via      252 261 266
G proteins, $G_{\alpha}$ , switch regions      257—259 258F
G proteins, $G_{\alpha}$ , three-dimensional structure      254—257 264
G proteins, $G_{\beta}$       253
G proteins, $G_{\beta}$ , binding to GTPase domain of $G_{\alpha}$       263—264
G proteins, $G_{\beta}$ , seven-blade propeller fold and WD units      261—263
G proteins, $G_{\gamma}$       252
G proteins, $G_{\gamma}$ , structure      263
G proteins, activated ( $G_{\alpha}$ -GTP)      253 254 256
G proteins, activated ( $G_{\alpha}$ -GTP), structure      253 253F
G proteins, activation      252 264
G proteins, activation by rhodopsin      265
G proteins, adenylate cyclase activation      253 253F
G proteins, definition      252
G proteins, genes      252
G proteins, heterodimer ( $G_{\beta\gamma}$ )      253
G proteins, heterodimer ( $G_{\beta\gamma}$ ), phosducin binding in rod cells      265—266 266F
G proteins, heterodimer ( $G_{\beta\gamma}$ ), regulation by phosducin      265 266
G proteins, heterodimer ( $G_{\beta\gamma}$ ), structure      262 262F 263 263F 264
G proteins, heterotrimer ( $G_{\alpha\beta\gamma}$ )      252 253 253F
G proteins, heterotrimer ( $G_{\alpha\beta\gamma}$ ), $G_{\alpha}$ binding to $G_{\beta}$       263—264
G proteins, heterotrimer ( $G_{\alpha\beta\gamma}$ ), regulators      266
G proteins, heterotrimer ( $G_{\alpha\beta\gamma}$ ), structure      262—263
G proteins, inactive ( $G_{\alpha\beta\gamma}$ )      253 253F
G proteins, physiological processed mediated by      252T
G proteins, signal transduction      254—264
G proteins, subunits      252
G proteins, subunits, amino acid residues      261 (see also “Transducin”)
G-actin      293 293F
GAL4      187—189
GAL4, amino acids      187
GAL4, dimerization regions      187 190
GAL4, DNA binding, linker region role      189
GAL4, DNA-binding domain      187F
GAL4, DNA-binding domain, binuclear zinc cluster      187—188 188F
GAL4, domain swapping with PPR1      190 190F
GAL4, upstream-activating sequence (UAS)      188
GAL4, zinc cluster regions      187—188 188F
GAL4, zinc cluster regions, binding to enhancer (CCG triplet)      188—189 189F 191
GAP (GTPase-activating protein)      254 261
GCN4      36 175 191
GCN4, amino acid sequence      192F 193 194F
GCN4, DNA binding, nucleotide sequence      194 194F
GCN4, DNA binding, specific and nonspecific contacts      194—196
GCN4, DNA recognition sites      194 194F
GCN4, DNA-binding domain      194 195F
GCN4, leucine zipper binding to DNA      193—194
GDP, GTP hydrolysis to      252 260
Gelatin      285
Gene control, lysogeny and lytic cycle      129—130
Gene duplication, $\gamma$ -crystallin Greek key motifs and      76
Gene duplication, antibodies, T-cell receptor and MHC      300
Gene duplication, chymotrypsin evolution      212
Gene duplication, enzyme evolution      55
Gene duplication, immunoglobulin evolution      301
Gene expression, regulation      151
Gene expression, regulation, eucaryotes      159
Gene expression, regulation, procaryotes      159
Gene fusion, double $\alpha/\beta$ barrel formation      52—53 52F
Genetic code, amino acid side chains      4—5
Genetic economy, viruses      327 330
Genome organization, enzyme differences and      53
Gilbert, Walter      76
GLI      179 180F
Globin family      42
Globin fold      22F 35 40 401
Globin fold, conservation during evolution      41—42
Globin, hydrophobic interior      42—43
Globin, low sequence homology between      42—43
Globular proteins      90—91
Globular proteins, $\alpha$ helix      15
Globular proteins, coiled coils in      287
Globular proteins, turnover and flexibility      91
Glucagon, NMR and x-ray crystallography comparison      391
Glucocorticoid receptor      181—183 182F
Glucocorticoid receptor, $\alpha$ helix in zinc motif      184—185
Glucocorticoid receptor, dimer binding to DNA      183—184
Glucocorticoid receptor, DNA-binding domain      181—183 181F
Glucocorticoid receptor, DNA-binding domain, amino acid sequence      182F
Glucocorticoid receptor, DNA-binding domain, sequence-specific interactions      184—185 185F
Glucocorticoid receptor, function of two zinc ions      185
Glucocorticoid receptor, recognition helix      184—185
Glucocorticoid receptor, structure      182F 183 183F
Glucocorticoid response element (GRE)      183
Glutamic acid, side chain in ribonucleotide reductase      11 11F
Glutamic acid, structure      6F
Glutamine, GTP hydrolysis mechanism      260 260F
Glutamine, lysozyme-antilysozyme complex      310F
Glutamine, parvalbumin calcium-binding motif      25
Glutamine, recognition helix of repressor and Cro      139 141
Glutamine, structure      6F
Gly-Gly-X repeats      289 290
Glycine in silk fibroins      289
Glycine, collagen      285 286
Glycine, conformations      9—10
Glycine, conformations in folded structures      356
Glycine, effect on protein stability      356—357
Glycine, p53 mutations      167—168
Glycine, side chain      5 7F
Glycine, specificity of serine proteinases      213
Glycine, structure      7F
Glycolysis      114
Glycolytic enzymes      47
Goldman, A.      245
Goldsmith, Elizabeth      111
Greek key motif      27 27F 73F
Greek key motif in antiparallel $\beta$ structures      72—74
Greek key motif, $\gamma$ -crystallin      74—75 75F 76
Greek key motif, $\gamma$ -crystallin, evolution      76
Greek key motif, alphaviruses core proteins      341
Greek key motif, chymotrypsin      211 211F
Greek key motif, complex arrangements      31 31F
Greek key motif, constant domain of immunoglobulin      304 304F
Greek key motif, jelly roll barrel formation      77 (see also “Jelly roll motifs”)
GroEL      100—102
GroEL, ATP complex      103
GroEL, cylindrical structure      100—102 100F
GroEL, cylindrical structure, model      101F
GroEL, domains      100—101 101F
GroEL, domains, apical      100 101F 102
GroEL, domains, equatorial      100 101F
GroEL, domains, intermediate      101F 102
GroEL, GroES binding      101F 102—104
GroEL, model      101F
GroEL-GroES complex      102—104
GroEL-GroES complex, functional cycle      104F

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