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

GroEL-GroES complex, protein folding inside      104
GroES      100
GroES, binding to GroEL      101F 102
GroES, subunits and structure      102 103F
Growth hormone      37 38F 267—270
Growth hormone receptor      267
Growth hormone receptor as model for erythropoietin receptor agonist      364—365
Growth hormone receptor, 1:1 complex      268—269
Growth hormone receptor, 1:2 complex      268
Growth hormone receptor, C-terminal regions      267 268
Growth hormone receptor, dimerization, induced by growth hormone      267—268 269
Growth hormone receptor, dimerization, sequential process      268—269
Growth hormone receptor, extracellular domains      267 267F
Growth hormone receptor, ligand-binding site      268
Growth hormone, binding to prolactin receptor      269—270 269F 270F 271F
Growth hormone, dimerization of receptor induced by      267—268 269
Growth hormone, four-helix bundle structure      37 38F 267 267F
Growth hormone, receptor complex      268F 365
GTP hydrolysis      252
GTP hydrolysis by $G_{\alpha}$       259—260 260F 261F
GTP hydrolysis by Ras      260—261
GTP hydrolysis, mechanism      259—261 260F 261F
GTP hydrolysis, prevention by cholera toxin      254
GTP hydrolysis, rate, GAP and RGS effect      261
GTP hydrolysis, regulators (RGS)      252 261 266
GTP hydrolyzing enzymes      255 (see also “G proteins “GTPase” “Ras
GTP, G protein activation      252
GTP, hydrolysis      see “GTP hydrolysis”
GTP, linking to Ras proteins      255 255F
GTP-binding proteins      254 (see also “G proteins”)
GTPase      254
GTPase, G proteins as      252 259—260
GTPase, mechanism of GTP hydrolysis      259—261 260F 261F
GTPase, transducin $G_{\alpha}$       256 256F
GTPase-activating protein (GAP)      254 261
Guanine in DNA, hydrogen bonds      123F
Guanine, G proteins binding      252
Guanine, zinc finger motif binding      181
Guanyl cyclases, transmembrane      271
H subunit, photosynthetic reaction center      235 236—237
Haemophilus influenzae, genome      55
Hairpin $\beta$ motif      26—27 26F
Hairpin $\beta$ motif, chymotrypsin      211 211F
Hairpin $\beta$ motif, complex motif arrangement      30—31 31F
Hairpin $\beta$ motif, hemagglutinin and pH changes      82F
Hairpin loops      21 21F
Hairpin loops, reverse turns      21—22 21F
Halobacterium halobium      226
Handedness, $\alpha$ helix      16 285
Handedness, $\beta-\alpha-\beta$ motif      28 48 49F 217
Handedness, amino acids      5
Handedness, polyproline type 11 (left-handed)      285
Hanging-drop method      375 376F
Haptens      308
Haptens, antigen-binding site      308—309 309F
Hardman, Karl      23
Harrison, Stephen      136 169 187 190 276 319 331 342
Hartl, Ulrich      104
Hck      275 276
Heat-shock proteins (Hsps)      100
Heavy chains      see under “Immunoglobulin(s)”
Heavy metals, in x-ray diffraction      380—381
Helical wheel      17T
Helix, $\alpha$       see “ $\alpha$ helix (helices)”
Helix-loop-helix (HLH) motif      24 39 196—197
Helix-loop-helix (HLH) motif, amino acid sequences      201F
Helix-loop-helix (HLH) motif, calcium binding      24 25F
Helix-loop-helix (HLH) motif, consensus sequence recognized      197 199 201
Helix-loop-helix (HLH) motif, homodimer and heterodimers      196—197 196F
Helix-loop-helix (HLH) motif, transcription factors      see “b/HLH transcription factors”
Helix-turn-helix motif      24 25F 129—149 133 134F 159
Helix-turn-helix motif, catabolite gene activating protein (CAP)      146 146F
Helix-turn-helix motif, Cro proteins      132 134F
Helix-turn-helix motif, DNA binding      133 134F
Helix-turn-helix motif, homeodomain similarity      160 161F
Helix-turn-helix motif, lac repressor      144 145F
Helix-turn-helix motif, lambda repressor      133 133F
Helix-turn-helix motif, phage 434 repressor and Cro protein      137
Helix-turn-helix motif, POU region binding to DNA      164—166 164F 165F
Helix-turn-helix motif, trp repressor      142 142F
Helix-turn-helix motif, two tandemly orientated in POU region      164—166 164F
Hemagglutinin      77
Hemagglutinin as membrane fusogen      80
Hemagglutinin as membrane fusogen, pH effect      82
Hemagglutinin, and       79 79F
Hemagglutinin, inhibitors      80
Hemagglutinin, jelly roll motif      80 81F
Hemagglutinin, low and high pH forms      82—83 82F 83F
Hemagglutinin, polypeptide chains      78F 79
Hemagglutinin, sialic acid binding domain      80 81F
Hemagglutinin, subunit structure      79 79F
Hemagglutinin, subunit structure, pH change effect      81—84
Hemagglutinin, subunit structure, stem and tip      79—80 80F
Hemagglutinin, synthesis      79
Hemagglutinin, trimer molecule      79—80
Heme pocket      43
Heme pocket, evolutionary conservation      43
Hemoglobin, concentrations      43
Hemoglobin, globin fold in      40
Hemoglobin, polymerization in sickle-cell anemia      44
Hemoglobin, sickle-cell      see “Sickle-cell hemoglobin”
Hemoglobin, structure      43 44F
Hen egg-white lysozyme, folding pathways      95—96 95F
Henderson, Richard      226
Hendrickson, Wayne      319 381
Heparin      113
Heptad repeats      36 36F 192 286
Heptad repeats in fibrous proteins      287
Herzberg, Osnat      26
Heterodimers, Fos-Jun      192—193
Heterodimers, HLH motif      196—197 196F
Heterodimers, leucine zippers      192—193 193F
Heterodimers, Myc with Max      199
Heterodimers, retinoid X receptor      185—186
Heterodimers, transcription factor binding to DNA      163 163F
Hexokinase      58F 293
Hinge helix, lac repressor      144
Hinge region, immunoglobulins      303 312 312F
Histidine in LH1 light-harvesting complex      242
Histidine in LH2 light-harvesting complex      241 241F
Histidine in serine proteinases      209
Histidine, barnase stabilization      357—358
Histidine, DNA binding domain of glucocorticoid receptor      181—182
Histidine, side chain in alcohol dehydrogenase      11 11F
Histidine, structure      7F
Histidine, substrate-assisted catalysis      218
Histidine, zinc finger motif      176 176F
Histidine, zinc finger motif, interaction with DNA      179 179F
HIV, CD4 receptor      319
HIV, Nef protein      275 276F
HIV-1 protease, L- and D- forms      9
HLA-A2      312 313 313F
HLH motif      see “Helix-loop-helix (HLH) motif”
Hogle, James      333
Hol, Wim      111
Holmes, Ken      255 292 296
Homeobox      159
Homeodomain proteins      159—160 160
Homeodomain proteins, definition      159
Homeodomain proteins, evolutionary role      159—160
Homeodomain proteins, monomer binding to DNA      160—162 161F
Homeodomains      160
Homeodomains, amino acid sequences      160 162 162F
Homeodomains, conserved residues      161
Homeodomains, engrailed      162F 165
Homeodomains, function in vivo      166
Homeodomains, helix-turn-helix motif comparison      160 161F
Homeodomains, recognition helix      161
Homeodomains, selectivity      162—164
Homeodomains, structure      160 160F

Homeotic transformations      159
Homodimerization      202
Homologous proteins      29 348—350
Homologous proteins, conserved structural cores and variable loops      349—350 349F
Homologous proteins, definition      348
Homologous proteins, multiple alignment, secondary structure prediction      351—352
Homologous proteins, similar structure and function      348
Homology, definition      348
Hormone-response elements      181
Horseshoe folds      47 55
Horseshoe folds, leucine-rich motifs in      55—56
Horwich, Arthur      100
hsc70      293
Hsp 10      100
Hsp 60      100
Hsp 70 (DnaK)      100
Huber, Robert      26 26F 111 210 235
Human growth hormone      see “Growth hormone”
Human lymphocyte antigen (HLA), HLA-A2      312 313 313F
Human rhinovirus      333 336F
Human rhinovirus, antiviral drug design      337—338 337F 338F
Human rhinovirus, ICAM-1 receptor      338
Human rhinovirus, “canyons” in VP1      337 337F 338
Huxley, A.F.      292
Huxley, H.E.      292 293
Hydrogen atoms, in NMR      387
Hydrogen bonds in $\alpha$ helix      15
Hydrogen bonds in $\beta$ strands      19
Hydrogen bonds, $G_{\alpha}$ activation      257 259F
Hydrogen bonds, acceptors and donors in DNA      125
Hydrogen bonds, B-DNA-protein interactions      124—125
Hydrogen bonds, jelly roll motif      78
Hydrogen bonds, mixed $\beta$ sheet      20 20F
Hydrogen bonds, nonspecific protein-DNA interactions      139—140 140F
Hydrogen bonds, subtilisin      217
Hydrogen bonds, TATA box and TBP binding      157 158
Hydrogen bonds, triple helix collagen      286 286F
Hydrogen bonds, zinc finger motif      177
Hydropathy index      245
Hydropathy plots      245 246F
Hydropathy plots, photosynthetic reaction center      245 246 246F
Hydrophilic regions, membrane proteins      223 223F
Hydrophilic residues in $\alpha$ domains      35
Hydrophilic residues in $\alpha$ helix      17
Hydrophobic core      14
Hydrophobic core, $\alpha$ domains      35 42—43
Hydrophobic core, formation      14
Hydrophobic core, T4 lysozyme      358
Hydrophobic interaaions, TATA box and TBP      157—158
Hydrophobic residues, in $\alpha$ helix      17
Hydrophobic side chains      see “Side chains”
Hydrophobicity, light-harvesting complex      242
Hydrophobicity, porins      231
Hydrophobicity, scales      245 245T
Hydrophobicity, transmembrane regions      223
Hydroxyproline, in collagen      284
Hypervariable regions, immunoglobulins      301 302F 305—306 349
Hypervariable regions, immunoglobulins, antigen-binding site      306—308 306F
Hypervariable regions, immunoglobulins, antigen-binding site, formation      306—308 306F 307F 308F
Hypervariable regions, immunoglobulins, conformations      305—306
Hypervariable regions, immunoglobulins, loop structure      305—306 306F
Hypervariable regions, immunoglobulins, modeling      349
Hypervariable regions, immunoglobulins, space-filling model      308F (see also “Complementarity determining regions”)
Hypervariable regions, T-cell receptor      316 317 318F
ICAM—1      338
Icosahedral symmetry      327—328 328F
Icosahedral symmetry, viruses      327 327F
icosahedron      327—328 328F
Icosahedron, asymmetric units      328 328F
Icosahedron, quasi-equivalent packing      330—331
Icosahedron, satellite tobacco necrosis virus      329
Icosahedron, symmetry      327—328
Icosahedron, triangulation numbers (T)      330
IgG      see “Immunoglobulin G (IgG)”
IGP-synthase      52
Image plates      377
Immune system      299—323
Immunoglobulin A (IgA)      301F
Immunoglobulin D (IgD)      301F
Immunoglobulin E (IgE)      301F
Immunoglobulin fold      168 304 304—305
Immunoglobulin fold in transcription factors      168—169
Immunoglobulin fold, antiparallel $\beta$ sheets      304—305 304F
Immunoglobulin G (IgG)      301 302
Immunoglobulin G (IgG), cleavage      304F
Immunoglobulin G (IgG), crystallization      312
Immunoglobulin M (IgM)      302
Immunoglobulin M (IgM), structure      301F
Immunoglobulin(s)      299
Immunoglobulin(s), antigen recognition      315
Immunoglobulin(s), antigen-binding site      see “Antigen-binding site”
Immunoglobulin(s), class-switching      302
Immunoglobulin(s), conformational flexibility      312 312F
Immunoglobulin(s), constant domains      301 301F 302
Immunoglobulin(s), constant domains, association in antigen-binding site      307 307F
Immunoglobulin(s), constant domains, comparison with variant domains      305 305F
Immunoglobulin(s), constant domains, globular units      306 306F
Immunoglobulin(s), constant domains, structure      304 304F
Immunoglobulin(s), diversity      302—303
Immunoglobulin(s), domains      301 301F 302 302F
Immunoglobulin(s), domains, classification      318—319
Immunoglobulin(s), evolution      301
Immunoglobulin(s), genetic recombination      302 302F 303F
Immunoglobulin(s), heavy chain      300—301
Immunoglobulin(s), heavy chain, antigen-binding site formation      306—308 306F
Immunoglobulin(s), heavy chain, CDR3 and CDR2      311
Immunoglobulin(s), heavy chain, diversity generation      302
Immunoglobulin(s), heavy chain, genes      302
Immunoglobulin(s), hinge region      303 312 312F
Immunoglobulin(s), hypervariable regions      see “Hypervariable regions”
Immunoglobulin(s), light chain      300—301
Immunoglobulin(s), light chain, antigen-binding site formation      306—308 306F
Immunoglobulin(s), light chain, CDR2      311
Immunoglobulin(s), light chain, diversity generation      302—303
Immunoglobulin(s), structure      301F
Immunoglobulin(s), V-D-J joining process      302 303F
Immunoglobulin(s), variable domains      301 301F 302F 305 305F
Immunoglobulin(s), variable domains, association in antigen-binding site      307—308 307F
Immunoglobulin(s), variable domains, globular units      306 306F
Immunoglobulin(s), variable domains, hypervariable regions in loops      305—306
Immunoglobulin-like domain      300
Immunosuppression, peptidyl, prolylisomerases in      98
Indoleglycerol phosphate (IGP) synthase      52—53 53F
Induced fit, ligand binding theory      114
Influenza virus      70
Influenza virus, binding site      80
Influenza virus, drug design targets      80
Influenza virus, hemagglutinin      see “Hemagglutinin”
Influenza virus, infection initiation      80 82
Influenza virus, neuraminidase      see “Neuraminidase”
Influenza virus, progeny and release      79
Influenza virus, protease treatment      79
Insulin, disulfide bridges      8
Interdomain movements      109—110
Intermediate filaments      287 287F
Intermediate filaments, construction model      287F
Inverse folding problem      353
ion channels      232—234 251
Ion channels, definition      232 (see also “Potassium channels”)
Iron atom, in photosynthetic reaction center      236 238
Iron in ribonucleotide reductase      11 11F
Iron, functions      11
Isaacs, Neil      241
Isoleucine, binding to SH2 domain      274
Isoleucine, Nef binding to SH3 domain      275
Isoleucine, structure      6F
Isoleucine, x-ray diffraction data      382
Isomerization      227F
Isomerization, proline residues      98—99 99F
Isomerization, retinal      227F 228 229F

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