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

Isotypes      300
Jacob, Francois      143
James, Michael      210
Jansonius, Hans      52
Janus protein      369T 370
Jelinski, Lynn      290
Jelly roll barrel in two $\beta$ 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, $\alpha/\beta$ -horseshoe fold      55—56
Levinthal, Cyrus      91
Lewis, Mitchell      143
LH1 and LH2      see “Light-harvesting complexes”
Ligand-binding sites, $\alpha$ 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 $G_{\alpha}$       256
Lipid-binding proteins      70
Lipids, membrane      223 246—247 253
Lipscomb, William      60
Loop regions      21—22
Loop regions in $\alpha/\beta$ barrels      49
Loop regions in $\beta-\alpha-\beta$ 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, $G_{\alpha}$ 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 $\alpha 1$       162
Mat $\alpha 2$ gene, homeodomain      162 162F
Mat $\alpha 2$ repressor      160
Mat $\alpha 2$ -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, $\alpha$ 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, $\alpha/\beta$ , 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, $\beta-\alpha-\beta$ motif      see “ $\beta-\alpha-\beta$ motif”
Motifs, combined into domains      29 30
Motifs, Greek key      see “Greek key motif”
Motifs, hairpin $\beta$       see “Hairpin $\beta$ motif”
Motifs, jelly roll      see “Jelly roll motifs”
Motifs, simple      24—26
Motifs, simple, combination into complex motifs      30—31 (see also “ $\alpha$ 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, $\alpha$ 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 $\alpha$ 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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