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

Sliding filament model      291 291F
Smith, George      361
Snake venom      26 26F
Solar cells      240 244
Somatic hypermutation      303
Specificity constant      206
Specificity pocket      209
Specificity pocket, chymotrypsin      211 211F
Specificity pocket, engineered mutations      213—215
Specificity pocket, hydrophobic, in subtilisin      217
Specificity pocket, preferential cleavage conferred by side chains      212—213
Spectrin      36
Spider dragline fibers      289
Spider silk      289—290 290F
Spiders’ webs      283
Spin, of nuclei      387
Spiral      see “Helical wheel”
Spongiform encephalopathies      113 288
Sprang, Stephen      256 262
Src tyrosine kinase      275—277
Src tyrosine kinase, active and inactive forms      278
Src tyrosine kinase, helix $\alpha C$       278
Src tyrosine kinase, phosphorylation      275 276
Src tyrosine kinase, regulation      278F
Src tyrosine kinase, SH2 domain      273F 275—277
Src tyrosine kinase, SH2 domain, linker region with N-terminal domain      277
Src tyrosine kinase, SH3 domain      275—277
Src tyrosine kinase, structure      276F 277F
Src-homology-2      see “SH2 domain”
Src-homology-3      see “SH3 domain”
Stability in protein engineering      see “Protein engineering”
Staggered conformations      10—11 10F
Staphylococcus nuclease      27 27F
Steitz, Thomas      58F 146 245
Stemmer, Willem      365
Stereochemical data, prediction of secondary structure      351
Strandberg, Bror      329
Streptomyces lividans      232
Structural hierarchy, of proteins      28—29
Stuart, David      333
Substrate specificity, chymotrypsin family      212—213
Substrate specificity, trypsin mutation      213 215
Substrate-assisted catalysis      218—219 218F
Substrates, transition state      207 207F
Subtilisin      28F 215
Subtilisin, $\beta-\alpha-\beta$ motif and handedness      217
Subtilisin, active sites      216—217 216F
Subtilisin, amino acids      215
Subtilisin, catalysis without catalytic triad      217—218
Subtilisin, catalytic triad      216 217
Subtilisin, evolution      210
Subtilisin, protein engineering      215 217 219
Subtilisin, structural anomaly and functional effects      217
Subtilisin, structure      215 216F
Subtilisin, substrate-assisted catalysis      218—219
Subtilisin, transition-state stabilization      217
Sugar-binding proteins      62F 6363F
Superbarrel, neuraminidase      72
Superfamily, chymotrypsin      210 212
Superfamily, retinol-binding protein (RBP)      70
Superoxide dismutase (SOD)      67F
Supersaturated solutions      375
Supersecondary structures      see “Motifs”
SV40      326 341—343
SV40, structure      342 342F
Swinging cross-bridge model      292 292F 296F
Swinging cross-bridge model, myosin structure supporting      295—296
Switch points, topological      59 60
Switch regions      256
Switch regions, $G_{\alpha}$ activation      257—259
Switch regions, myosin S1 fragment      294
Synchrotrons      376 377 384
T (tense) state      113—114
T-cell receptors (TCR)      299 300 316—317
T-cell receptors (TCR), antigen-binding site      317F
T-cell receptors (TCR), gene rearrangements      316F 317
T-cell receptors (TCR), hypervariable regions      316 317 318F
T-cell receptors (TCR), MHC-peptide complexes as ligands      318 318F
T-cell receptors (TCR), variable and constant regions      316—317
T-cells, activation      312—313
T-loop      108 109F
T4 bacteriophage      see “Bacteriophage T4”
Tandem repeats, leucine-rich in in $\alpha/\beta$ -horseshoe folds      56
Tandem repeats, retinoid X receptor recognizing      185—186
TATA box      151 151F 155
TATA box, consensus sequence      154F
TATA box, DNA deformation      155—157
TATA box, TBP binding, hydrogen bonds      157 158
TATA box, TBP binding, hydrophobic interactions      157—158
TATA box, TBP binding, sequence-specific      157—158 157F
TATA box, TBP complexes with      154
TATA box, TBP preference for      157 158
TATA box-binding protein (TBP)      151 152 152F 153—154
TATA box-binding protein (TBP), amino acid sequences      153
TATA box-binding protein (TBP), binding to minor groove of DNA      155—157 156F
TATA box-binding protein (TBP), C-terminal domain      153—154
TATA box-binding protein (TBP), DNA deformation after binding      155—157 156F
TATA box-binding protein (TBP), DNA-binding sites as $\beta$ sheet      154
TATA box-binding protein (TBP), isolation      153
TATA box-binding protein (TBP), motifs      158
TATA box-binding protein (TBP), mutants      153—154
TATA box-binding protein (TBP), N-terminal segment      154
TATA box-binding protein (TBP), preference for TATA box      157 158
TATA box-binding protein (TBP), promoter complex      159
TATA box-binding protein (TBP), side chains      154 157
TATA box-binding protein (TBP), TATA box complexes      154
TATA box-binding protein (TBP), TFIIA and TFIIB binding      159
TATA box-binding protein (TBP), ubiquity      153—154
Taylor, Susan      278
TBP      see “TATA box-binding protein (TBP)”
TBP-associated factors (TAFs)      152 153
Temperature factor (B)      383
Temperature, melting (Tm)      354 356F
Tertiary structure of proteins      3F 28 29
Tertiary structure of proteins, local secondary structure imposed by      351
Tertiary structure of proteins, molten globular state      89
Tertiary structure of proteins, prediction, secondary structure knowledge required      350—351
Tertiary structure of proteins, protein engineering      347—348 (see also “Domains” “Motifs” “Three-dimensional
TFIIA      see “Transcription factor TFIIA”
Thioredoxin, NMR and x-rav crystallography comparison      391
Thioredoxin, phosducin homology      265—266
Thioredoxin, structure      20F 97
Threading methods      353—354
Three-dimensional model, homologous proteins      348
Three-dimensional structure of proteins      3 4
Three-dimensional structure of proteins, disulfide bridge stabilization of      8
Three-dimensional structure of proteins, prediction      89 349 349F
Three-dimensional structure of proteins, similar with different amino acid sequences      352 (see also “Domains” “Motifs” “Tertiary
three-dimensional structures      303—304 304F
Threonine, Ras and $G_{\alpha}$ proteins      256
Threonine, structure      6F
Thymine, in DNA, hydrogen bonds      123F
Thyroid hormone receptor      185 186F
TIM barrel      47 267
Tissue factor-factor Vila (TF-FVIIa)      361 362 362T
Titin      290—291
Tm (melting temperature)      354 356F
Tobacco mosaic virus      326F
Tobacco mosaic virus, coat protein      37
Tomato bushy stunt virus      331—332 332F
Tomato bushy stunt virus, capsid structure      331—332 332F
Tomato bushy stunt virus, jelly roll structure      335F
Tomato bushy stunt virus, S and $\beta$ domains      332 332F
Tomato bushy stunt virus, size      332
Tomato bushy stunt virus, subnits recognizing RNA      332—333 333F
Topological switch points      59 60
Topology diagram      23
Topology diagram, $\alpha/\beta$ domains      48F
Topology diagram, $\beta-\alpha-\beta$ motif      28F
Topology diagram, $\gamma$ -crystallin      74F 75F

Topology diagram, carboxypeptidase      61F
Topology diagram, chymotrypsin      211F
Topology diagram, complex motifs      31 31F
Topology diagram, fibronectin type III domain      319F
Topology diagram, Greek key motifs      27F
Topology diagram, immunoglobulin      304F
Topology diagram, jelly roll motif      78F
Topology diagram, neuraminidase      71F
Topology diagram, open twisted $\alpha/\beta$ structures      58F
Topology diagram, pS3 DNA-binding domain      168
Topology diagram, Ras proteins      254F
Topology diagram, subtilisin      217F
Topology diagram, TATA box-binding protein      155F
Topology diagram, up-and-down $\beta$ barrels      68F
Topology diagram, uses and advantages      76
Trans-peptide      98 98F
trans-retinoic acid (RAR) receptor      185 186F
Transcription factor      151—174 175—203
Transcription factor GCN4      see “GCN4”
Transcription factor Oct-1      164F 165
Transcription factor PPR1      190—191 190F
Transcription factor TFIIA, binding to TBP and DNA      159
Transcription factor TFIIA, domains      159
Transcription factor TFIIB, binding to TBP and DNA      159
Transcription factor TFIIB, domains      159
Transcription factor TFIID      151 152 158
Transcription factor TFIIIA, zinc finger motifs      176 177
Transcription factor, classes      152
Transcription factor, definition      151
Transcription factor, domains      153
Transcription factor, eucaryotic      175 191
Transcription factor, evolution      202
Transcription factor, families      153 175—203
Transcription factor, functions of polypeptide chains      152—153
Transcription factor, genes encoding, cloning      153
Transcription factor, helix-loop-helix (HLH) family      39
Transcription factor, heterodimer binding to DNA      163 163F
Transcription factor, homeodomains      see “Homeodomains”
Transcription factor, immunoglobulin fold in      168—169
Transcription factor, leucine zipper motifs      191—193
Transcription factor, POU region      164F
Transcription factor, procaryotic      175
Transcription factor, selectivity, homeodomains      162—164
Transcription factor, zinc-containing motifs      see “Zinc-containing motifs”
Transcription, activation by CAP-induced DNA bending      146—147
Transcription, activation, model      152F
Transcription, activation, protein-protein interactions      152—153
Transcription, DNA elements involved      151F
Transcription, initiation complex      153
Transcription, initiation, TBP binding to TATA box and      158
Transcription, preinitiation complex      151 152 159
Transcription, regulation      152
Transcription, regulation, eucaryotes      151
Transducin      256
Transducin, $G_{\alpha}$ structure      256 256F
Transducin, $G_{\beta\gamma}$ structure      262 262F 263 263F
Transducin, activation by rhodopsin      265
Transition states      206
Transmembrane $\alpha$ helices      226—227
Transmembrane $\alpha$ helices, bacteriorhodopsin      226—227 226F
Transmembrane $\alpha$ helices, hydropathy plots      245 246F
Transmembrane $\alpha$ helices, LH2 light-harvesting complex      241 241F 242F
Transmembrane $\alpha$ helices, no specific interaction with membrane lipids      246—247
Transmembrane $\alpha$ helices, photosynthetic reaction center      244—245
Transmembrane $\alpha$ helices, prediction from amino acid sequences      244—245
Transmembrane $\alpha$ helices, subunits of photosynthetic reaction center      236—237 237F
Transmembrane enzyme-linked receptors      271
Transmembrane proteins, $\alpha$ helices      18
Transthyretin      288
Transthyretin, twisted $\beta$ helix      288 288F 289F
Triangulation numbers (T)      330
Triosephosphate isomerase, $\beta-\alpha-\beta$ motif      28 28F
Triosephosphate isomerase, $\beta-\alpha-\beta-\alpha$ motifs      30 30F
Triosephosphate isomerase, amino acids of $\beta$ strands      48 50T
Triosephosphate isomerase, structure      23F
Triosephosphate isomerase, TIM barrel structure      47
Troponin-C      24 26
Troponin-C, helical wheel      17T
trp repressor, conformational change effect      142—143
trp repressor, dimerization      142 142F
trp repressor, helix-turn-helix motif      142 142F
trp repressor, structure      142
trp repressor, tryptophan binding      142—143 143F
Trypsin, Asp 189-Lys mutation      215
Trypsin, kinetic data      214F
Trypsin, mutant, specificity pocket      214F
Trypsin, preferential cleavage sites      212 213 213F
Trypsin, specificity mechanism      209
Trypsin, specificity pocket      214F
Tryptophan, binding to trp repressor      142—143 143F
Tryptophan, operon      142
Tryptophan, structure      7F
Tryptophan, synthesis      142
TTK      179 180F
Tu, elongation factor      255
Tubulin      284
Tumor suppressor gene      166 (see also “p53”)
Tumorigenic mutations      166
Tumorigenic mutations, pS3 regions      170—171 170F
Turnover number ( $K_{cat}$ )      206
Two-dimensional crystals, membrane proteins      225—226 226F
Tyrosine kinase, receptor      270—271 271 272F
Tyrosine kinase, Src      see “Src tyrosine kinase”
Tyrosine kinase-associated receptors      270 271 272F
Tyrosine kinase-associated receptors, adaptor modules      272 272F
Tyrosine phosphatases      271
Tyrosine, structure      6F 59
Tyrosyl adenylate      60F
Tyrosyl-tRNA synthetase, domains      59—60 59F 60F
Tyrosyl-tRNA synthetase, side chains      61F
Tyrosyl-tRNA synthetase, tyrosine bound to      60 60F
Ubiquinone      236F
Ultraviolet light, Cro formation and lytic cycle      131 133
Unit cell      374
Unwin, Nigel      226
Up-and-down $\beta$ barrels      68 68—71 68F
Up-and-down $\beta$ barrels, porin channels      229—230 230F
Up-and-down $\beta$ barrels, SH3 domain      274 275F
Up-and-down $\beta$ sheets, in neuraminidase      70—71 71F
Upstream-activating sequence (UAS), GAL4      188
Urokinase      29F
Valegard, Karin      339
Valine, recognition helix of glucocorticoid receptor      184—185
Valine, staggered conformations      10—11 10F
Valine, structure      6F
Vibrio cholerae      254
Vimentin      287F
Viruses      325—345
Viruses, capsid      325 326
Viruses, capsid, polypeptide chains      325
Viruses, enveloped      325
Viruses, genomes      325 326 330
Viruses, infections      325
Viruses, jelly roll structures      335—337 335F 336F
Viruses, pentamers of coat protein      341—343 342F
Viruses, simplest      328—239
Viruses, sizes and shapes      326F
Viruses, spherical      325—345
Viruses, spherical, complex      329—331
Viruses, spherical, icosahedral symmetry      327 327F
Viruses, T=3 structure      330 330F
Viruses, T=3 structure, plant viruses      331—332 337
Viruses, T=4 structure      331 331F
Viruses, T=4 structure, Sindbis virus      341
Viruses, T=7 design      341—342 342F
Vitamin A (retinol)      68 68F 69F
Vitamin D receptor      185 186F
Vitamin D-resistant rickets      184
Vitronectin      113
Water in $G_{\alpha}$ activation      258

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