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

Proteinase inhibitors, affinity and specificity optimization      361—363
Proteinase, families      205—206 (see also “Serine proteinases”)
Proteolytic degradation, loop regions      22
Protofibrils      283
Protofilaments      283
Proton abstraction      54 54F
Proton channel, bacteriorhodopsin      227 228F
Proton pump      227
Proton pump, light-driven, bacteriorhodopsin as      227—228 229F
Psi ( $\psi$ ) angle      8 9 14
Psi ( $\psi$ ) angle, Ramachandran plot      9 9F 10
PSTAIRE helix      107F 108 108F 109F 278
Ptashne, Mark      135 190
Pulse amide hydrogen-deuterium exchange      95
PurR      143
PurR, repressor      144
pY+3 pocket      274 277
Pyrrol rings      238
Pyruvate kinase, domains and $\alpha/\beta$ barrel      51—52 51F
Quasi-equivalent packing, icosahedral subunits      330 343
Quasi-equivalent packing, T=3 plant viruses      331—332
Quaternary structure of proteins      3F 29
Quaternary structure of proteins, phosphofructokinase      116F
Quinone in photosynthetic reaction center      238 238F
Quinone in photosynthetic reaction center, and       238 238F 239
Quiocho, Florante      62 110
R (relaxed) state      113—114
R factors      383
Radio frequency (RF), in NMR      387
Ramachandran plot      9—10 9F 18 19 167
Random mutagenesis      359 359F
Ras protein      254—257
Ras protein, $G_{\alpha}$ comparison      256—257
Ras protein, diphosphate-binding loop (P-loop)      255—256
Ras protein, GTP hydrolysis mechanism      260—261
Ras protein, GTP linking via $\mathrm{Mg}^{2+}$       255 255F
Ras protein, loop regions      255—256
Ras protein, mutants      254 261
Ras protein, switch regions      256
Ras protein, three-dimensional structure      254—257 254F
Rayment, Ivan      294 295 342
RecA      131
Receptor tyrosine kinases      270
Receptor tyrosine kinases in cell growth and differentiation      271 272F
Receptor tyrosine kinases, activation and signaling      271
Receptors, enzyme-linked      see “Enzyme-linked receptors”
Receptors, extracellular domains      251 251F
Receptors, genes      252
Receptors, immunoglobulin-like domains      318—319
Receptors, organization      251F
Receptors, orientation importance      270
Receptors, peptide hormones      267
Receptors, transmembrane helices      252 (see also “Specific types”)
Recognition $\alpha$ helix      134
Recombinant DNA techniques      3 252 375
Recombinant DNA techniques, Multiwavelength Anomalous Diffraction method      381
Recombination      365—366
Recombination, immunoglobulin genes      302 302F 303F
Reflection angle      378 379F
Regan, Lynne      369
REL-homology region      169
Repressor proteins      125 129
Repressor proteins as activator for own synthesis      130F 131
Repressor proteins, action in genetic switch region      130—131 130F
Repressor proteins, actions/functions      130—131
Repressor proteins, differential binding to operator sites      140—141
Repressor proteins, dimerization      132—133 133F
Repressor proteins, dimers      131 132
Repressor proteins, DNA-binding domain      132—133 133F
Repressor proteins, DNA-binding, allosteric control      142
Repressor proteins, DNA-binding, Cro protein and DNA      134—135
Repressor proteins, DNA-binding, phage 434      136—137 137 137F
Repressor proteins, DNA-binding, phage 434 and P22      135 136F
Repressor proteins, lac      see “Lac repressor”
Repressor proteins, Mat $\alpha 2$       160
Repressor proteins, met      175
Repressor proteins, repression of Cro gene      130
Repressor proteins, summary      141—142
Repressor proteins, trp      see “trp repressor” (see also “Bacteriophage lambda”)
Restriction enzymes      125
Retinal      226
Retinal, binding to bacteriorhodopsin      227
Retinal, isomerization      227F 228 229F
Retinal, trans state      228 229F
Retinoic acid receptor      181 181F
Retinoid X receptor      185—186
Retinol      68 69F
Retinol-binding protein (RBP), amino acid sequence      69—70 70F
Retinol-binding protein (RBP), binding site for retinol      69F
Retinol-binding protein (RBP), structure      68F
Retinol-binding protein (RBP), superfamily      70
Retinol-binding protein (RBP), synthesis      68—69
Retinol-binding protein (RBP), up-and-down $\beta$ barrels      68—69 68F
RGS (Regulators of GTP hydrolysis)      252 261 266
Rhinovirus      see “Human rhinovirus”
Rhinoviruses      333
Rhodobacter capsulatus. porins      229 230F
Rhodobacter sphaeroides      236 246F 247F
Rhodopsendomonas acidophila      240F 241
Rhodopsin      265
Rhodospirillum molischianum      241
Rhodospirillum rubrum      243F
Rhvdopseudomonas viridis      235 236
Ribonuclease inhibitor      47
Ribonuclease inhibitor, horseshoe folds      55 56F
Ribonuclease, barnase, folding      94—95 94F
Ribonucleotide reductase, iron in      11 11F
Ribulose bisphosphate carboxylase (RuBisCo)      see “RuBisCo”
Rich, Alexander      285
Richardson, Jane      23 23F 25F
Richmond, Tim      196
Rigor mortis      295 296
RNA phage      339
RNA polymerase I      151
RNA polymerase II      151 152
RNA polymerase III      151
RNA polymerase, classes      151
RNA, bacteriophage MS2 packaging      339—340 340F
RNA, virus capsid units recognizing      332—333 333F
RNA-binding protein, ROP      see “ROP”
Rod cells      265
Rod cells, light-adapted and dark-adapted      265
Rop protein      38—39 39F 196
Rop protein, amino acid sequence      369T
Rossman fold      47 115
Rossmann, Michael      47 333 337 341
Rotamers      11 349
Rotamers, libraries      11
Rotating anode x-ray generators      376
Rous sarcoma virus      271
RuBisCo, active site      53F
RuBisCo, crystals      374F
Rutter, William      213
Salt bridges      36 37F
Salt bridges, $G_{\alpha}$ activation      258F 259
Sander, Chris      351
Sarcomeres      291F
Satellite tobacco necrosis virus      326F 329 329F
Satellite tobacco necrosis virus, coat      336F
Satellite tobacco necrosis virus, jelly roll structure      336F
Satellite viruses      329
Scaffolds, structural, homologous proteins      349
Scaffolds, structural, Kunitz domains of LACI-D1 and APPI      362
Scaffolds, structural, size reduction with full function      363—364
Scattering of electrons      378
Scattering of x-rays, anomalous      381
Schematic diagrams      22—23
Schematic diagrams, $G_{\alpha\beta\gamma}$ complex      264F
Schematic diagrams, $G_{\beta\gamma}$ from transducin      262F
Schematic diagrams, $G_{\beta}$ and WD repeat      263F

Schematic diagrams, $\alpha/\beta$ domains      48F
Schematic diagrams, $\beta$ sheet, antiparallel      18F
Schematic diagrams, $\beta$ sheet, parallel      19F
Schematic diagrams, $\beta-\alpha-\beta$ motif      28F
Schematic diagrams, $\gamma$ -crystallin      74F 75F
Schematic diagrams, Antennapedia homeodomains      160F
Schematic diagrams, arabinose-binding protein      62F 63F
Schematic diagrams, B-DNA      121F
Schematic diagrams, bacterial muramidase      39F
Schematic diagrams, bovine pancreatic trypsin inhibitor (BPT1)      96F
Schematic diagrams, carboxypepudase      61F
Schematic diagrams, CDK2      106
Schematic diagrams, chymotrypsin      210F
Schematic diagrams, coiled-coil $\alpha$ helix      35F 36F
Schematic diagrams, DNA-binding domain of glucocorticoid receptor      182F
Schematic diagrams, four-helix bundle      38F
Schematic diagrams, globin fold      40F
Schematic diagrams, GroEL      100F 101F
Schematic diagrams, GroES      103F
Schematic diagrams, hemagglutinin      78F 82F
Schematic diagrams, hydrogen bonding in collagen      286F
Schematic diagrams, immunoglobulins      301F 308F
Schematic diagrams, immunoglobulins, constant and variable domains      307F 308F
Schematic diagrams, ion pore of channel      233F
Schematic diagrams, major and minor grooves of DNA      122F 123F
Schematic diagrams, Max binding to DNA      200F
Schematic diagrams, MHC molecules      313F
Schematic diagrams, MyoD binding to DNA      198F
Schematic diagrams, myosin      294F
Schematic diagrams, neuraminidase      71F 72F
Schematic diagrams, open twisted $\alpha/\beta$ structures      58F
Schematic diagrams, ovalbumin      111F
Schematic diagrams, P helix      84F 85F 86F
Schematic diagrams, p53 DNA-binding domain      168F
Schematic diagrams, p53 oligomerization domain      167
Schematic diagrams, phosphofructokinase      115F
Schematic diagrams, Ras proteins      254F
Schematic diagrams, representations in      23
Schematic diagrams, Rop molecule      39F
Schematic diagrams, serpin fold      111F
Schematic diagrams, SH2 domain      273F
Schematic diagrams, SH3 domain      275F
Schematic diagrams, specificity pockets of serine proteinases      213F
Schematic diagrams, subtilisin      216F
Schematic diagrams, SV40      343F
Schematic diagrams, TATA box-binding protein      155F
Schematic diagrams, transducin $G_{\alpha}$       256F
Schematic diagrams, up-and-down $\beta$ barrels      68F
Schematic diagrams, virus jelly roll barrels      336F
Schematic diagrams, zinc finger motif      176F
Schematic diagrams, zinc fingers of Zif 268      178F
Schematic diagrams, “knobs in holes” model      37F
Schematic model, transcriptional activation      152F
Schiff base      227 228 229F
Schulz, Georg      58F 229
Scissile bonds      209 213F
Scrapie      113
Second messengers      253
Secondary structure of proteins      3F 14 28 29 89
Secondary structure of proteins in prediction of tertiary structure      350—351
Secondary structure of proteins, formation during folding process      93
Secondary structure of proteins, local, imposed by tertiary structure      351
Secondary structure of proteins, motif formation      24—26
Secondary structure of proteins, prediction from amino acid sequences      352—353
Secondary structure of proteins, prediction from homologous proteins      351—352
Secondary structure of proteins, prediction, $\alpha$ helix (helices)      352
Secondary structure of proteins, x-ray crystallography and NMR      374—392 (see also “ $\alpha$ helix (helices)” “
Secretory pathway, proteins      5
Selenomethionine      381
Semliki Forest virus      340
Sequences      see “Amino acid sequence”
Sequential assignment, two-dimensional NMR      389—390
Sequential model      113
Serine in serine proteinases      209
Serine proteinases      205—221
Serine proteinases, active sites      211—212 211F 212F 361
Serine proteinases, domains      29F 210F 211F
Serine proteinases, essential structural features      209
Serine proteinases, evolution      210
Serine proteinases, inhibition by serpins      110—113
Serine proteinases, reaction mechanisms      208 208F “Subtilisin”)
Serine, structure      6F
Serine/threonine kinases      271
Serpell, Louise      288
Serpin fold      111 111F
Serpins      110—113
Serpins, active, cleaved and latent forms      112 112F
Serpins, serine proteinase inhibition mechanism      110—113
Serpins, structure      111—112 111F
SH2 domain      272 273—274
SH2 domain in Src tyrosine kinase      273F 275—277
SH2 domain, phosphotyrosine-containing regions binding      272 273—274 278
SH2 domain, pY+3 pocket      274 277
SH2 domain, structure      273F
SH3 domain      272 274—275 285
SH3 domain in Src tyrosine kinase      275—277
SH3 domain, Nef binding      275 275F 276F
SH3 domain, proline-rich regions binding      273 274—275
SH3 domain, structure      274 275F
Sialic acid, binding domain of hemagglutinin      80 81F
Sialic acid, chemical formula      80F
Sialic acid, hemagglutinin binding      80
Sialic acid, neuraminidase role      70—71
Sickle-cell anemia      43—45
Sickle-cell anemia, malaria resistance      44—45
Sickle-cell hemoglobin      43—45 44F
Sickle-cell hemoglobin, hydrophobic patch on surface      43 44F
Sickle-cell hemoglobin, mutation in      44F
Side chains      4 4F
Side chains, $\alpha$ helix      17
Side chains, alcohol dehydrogenase      11 11F
Side chains, antigen recognition in MHC molecules      314—315 316
Side chains, branched hydrophobic, in $\alpha/\beta$ barrels      49—51
Side chains, charged      5 6F
Side chains, conformation prediction      349
Side chains, energetically favourable      10—11
Side chains, hydrophobic      5 6F 14
Side chains, hydrophobic, $\alpha/\beta$ barrels      49—51
Side chains, hydrophobic, antiparallel $\beta$ structures      67
Side chains, hydrophobic, burying as event in protein folding      93
Side chains, hydrophobic, coiled-coil $\alpha$ helix      36 36F
Side chains, hydrophobicity scales      245
Side chains, interactions in leucine zippers      192 193F
Side chains, mutations, $\alpha$ helix movements accommodating      43
Side chains, number      4—5
Side chains, pectate lyase $\beta$ helix      85
Side chains, polar      5 6F
Side chains, polar in Xfin      177
Side chains, polar, porins      231
Side chains, ribonucleotide reductase      11 11F
Side chains, serine proteinase specificity      209
Side chains, staggered conformations      10—11 10F
Side chains, TATA box-binding protein      154 157
Side chains, tyrosyl-tRNA synthetase      61F
Sigler, Paul      100 154 159 169 183 185 256 262
Signal transduction      251—281
Signal transduction by G proteins      254—264 (see also “G proteins”)
Signal transduction, amplification by rhodopsin      265
Signal transduction, phosducin system      265—266
Signal transduction, protein modules as adaptors      272—273 (see also “SH2 domain” “SH3
Signal transduction, receptor tyrosine kinases      271
Signal transduction, tyrosine kinases      271
Signal-transducing receptors      251
Signal-transducing receptors, G proteins      see “G proteins”
Silk fibroins      289 290F
Silk fibroins, genes      289
Sindbis virus      340
Sindbis virus, core protein      341 341F
Sippl, Manfred      354
SLH (strand-loop-helix) motif      168F 171

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