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Lesk A.M. — Introduction to Protein Architecture
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Название: Introduction to Protein Architecture
Автор: Lesk A.M.
Аннотация: Written in a clear and engaging style, and profusely illustrated with superb computer graphics, Introduction to Protein Architecture is a textbook for second and third year undergraduate students and beginning post-graduate students, and will be of interest to all biological and medical scientists whose work touches on proteins.
The structures and functions of proteins unlock the secrets inherent in genomes, including the human genome. The emphasis of this book is on protein architecture, on proteins as three-dimensional patterns. A new field, bioinformatics, has grown up around gene and protein sequences and structures. It has captured the interest of many scientists for its intellectual challenges, its potential for useful applications, and promising scope for careers. This book introduces the use of the World Wide Web in bioinformatics.
Written by one of the leaders in this field, Introduction to Protein Architecture explains the general characteristics of proteins that underlie the very great variety of folding patterns observed in nature. For specialists in structural biology, it contains the core of what they need to know. For students and workers in related disciplines, undergraduates or beginning graduate students in biology, chemistry, medicine, bioinformatics, and related fields it contains what they will be able to apply to their own work. Topics treated include: Pattern and form in protein structure; The building blocks; The relationship between amino acid sequence and protein structure; Secondary, supersecondary and tertiary structure; Classifications and hierarchies of protein folding patterns; Protein evolution; How proteins change conformation (and why).
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Рубрика: Биология /
Статус предметного указателя: Готов указатель с номерами страниц
ed2k: ed2k stats
Год издания: 2001
Количество страниц: 347
Добавлена в каталог: 16.03.2007
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Предметный указатель
Myoglobin (sperm whale) [1A6N, 1MBD, 1MBO] 26 177 196
Myoglobin (sperm whale) [1A6N, 1MBD, 1MBO], B/E helix interface 144 203
Myoglobin (sperm whale) [1A6N, 1MBD, 1MBO], B/G helix interface 143
Myoglobin (sperm whale) [1A6N, 1MBD, 1MBO], oxy and deoxy forms 272
Myoglobin (sperm whale) [1A6N, 1MBD, 1MBO], oxy form 273
Myoglobin, alignment table 168—169
Myoglobin, evolution 166ff 195ff
Myoglobin, oxygen binding 271ff
Myoglobin, relationship to phycocyanin 200fF
Myosin (chicken) [2MYS], [1BR1], [1BR2] 275
Myosin, hinge motion 274
NAD-binding domain 27—28 151—152 217
NAD-binding domain, hydrogen-bonding pattern 218ff
NADP, binding 224
NADPH-cytochrome P450 reductase (rat) [1AMO] 133
Neurotoxin B (sea snake) [1NXB] 317
Neutral mutation 174
Neutron diffraction 110
Nuclear magnetic resonance (NMR) 37 40—42
Nuclear Overhauser effect 40
Nucleosome 3
Oncomodulin (rat) [1RRO] 310
Opsin 188ff
Ovalbumin (chicken) [1OVA] 293
Ovomucoid third domain (silver pheasant) [2OVO] 322
Packing 29—30
Packing, interior of -barrel 154—157 213—216
Pancreatic trypsin inhibitor (cow) [5PTI] 317
Papain 183
Papain (papaya) [9PAP] 178
PDB see “Protein Data Bank”
Pfam (multiple sequence alignments) 88 121
Phase problem 37—38
Phosphatidylinositol 3-kinase (human) [1PBW] 313
Phosphofructokinase (Bacillus stearothermophilus) [4PFK] 107
Phosphoglycerate kinase (yeast) [3PGK] 79
Phospholipase (cow) [1BP2] 81
Phospholipase (Taiwan cobra) [1POA] 312
Phospholipase (western diamondback rattlesnake) [1PP2] 314
Phosphotyrosine protein phosphatase (cow) [1PHR] 331
Photoactive yellow protein (Ectothiorhodospira halophila), -helix [2PHY] 65—66
Photosynthetic reaction centre 1
Photosynthetic reaction centre (Rhodopseudomonas viridis) [1PRC] 2 4—9
Phycocyanin (Mastigocladus laminosus), -chain 202
Phycocyanin (Mastigocladus laminosus), -chain, (B/E) helix contact 203
Phycocyanin, relation to globins 200ff
Plastocyanin 183ff
Plastocyanin (poplar leaf) [5PCY] 106 179
Plastocyanin, copper-binding site 105
Polyhedral model, of helix assembly 141
Polyproline II helix 62 67 68
Primary structure 70
Prion protein domain prp (mouse) [1AG2] 325
PROSITE 95
Proteasome 3
Protein conformation 100
Protein Data Bank 42ff 79
Protein denaturation 37
Protein engineering 18
Protein evolution 88
Protein folding 17 18 22—23 297ff
Protein G: third IgG-binding domain (streptococcus) [1IGD] 318
Protein structure classification 84—85 89 127ff
Protein structure prediction 18 90 94 97ff
Protein-nucleic acid complex 109—110 120 135
Proteinase (Rous sarcoma virus) [2RSP] 319
Proteinase b Streptomyces griseus [3SGB] 209
Proteinase b Streptomyces griseus [3SGB], domain 1 212
Proteinase specificity 30 211
Prothrombin (cow), kringle domain [2PF1] 159
PSI-BLAST 47
Quaternary structure 70
Quinone oxidoreductase (Escherichia coli), NAD-binding domain [1QOR] 224
R-factor 40
r-free 40
Ras-GTPase-activating domain of human pl20gap [1WER] 137
Reaction centre 1
Refinement of X-ray crystal structures 38
REI (human), Vk: domain [1REU] 236
Resolution 39
Retinol-binding protein (human) [1RBP] 107
Ribonuclease inhibitor (pig) [2BNH] 334
Ribonuclease Streptomyces aureofaciens [1RGE] 87
Ribonuclease T1 (Aspergillus oryzae) [2RNT] 82
Ribosomal protein L7/L12 (Escherichia coli) [1CTF] 83
Ribosomal protein S6 (Thermus thermophilus) [1RIS] 162
Ribosome 3
Ridges-into-grooves packing 142ff 197ff
Root-mean-square deviation 180
Rotamer 35
Rotamer library 35
Salt bridge 21—22
Sasisekharan-Ramakrishnan-Ramachandran plot 32 35 40—41 49 55 59 96 216 255
Scolexin 207
SCOP (Structural Classification of Proteins) 43 127ff 132
Secondary structure 49 70
Secondary structure, assignment 79—80
Serine proteinase 16 18
Serine proteinase, catalytic mechanism 205—206
Serine proteinase, evolution 201
Serine proteinase, hydrogen bonding pattern 210 215
Serine proteinase, specificity 211 213
Serine proteinase, viral 3C 207
Serpins (serine proteinase inhibitors) 290ff
Serpins (serine proteinase inhibitors), transition 291
Serum response factor, core fragment (human) [1SRS] 329
Shear number of -barrel 154 213
Sheet see “ -sheet”
Sickle-cell anemia 182
Signal sequence recognition protein FFH (Thermus aquaticus) [1FFH] 130
Signal-transduction protein CheY (Escherichia coli) [1CHN] 134
Signal-transduction protein CheY (Escherichia coli) [3CHY] 93
Single-nucleotide polymorphism (SNP) 182
Skn-1 (Caenorhabditis elegans) [1SKN] 120
SMART 88
SNP (single-nucleotide polymorphism) 182
Somatic mutation 237
Special pair 10
Staphylococcal nuclease [2SNS] 150
Streptococcal protein G B1 (immunoglobulin binding domain) [1PGA] 69 73
Streptomyces griseus proteinase b [3SGB] 209
Streptomyces griseus proteinase b [3SGB], domain 1 212
Structural genomics 16 18
Structure comparison 85
Sulphate-binding protein (S. typhimurium) [1SBP] 106
Superposition 86-87 101 104 185 251
Supersecondary structure 50 75—78
Surface area 27
Surfaces, interior and exterior of proteins 27
T-cell receptor (TCR) 247 261ff
T-cell receptor (TCR), canonical structures 262
T-cell receptor (TCR), interaction with MHC protein 263ff
T-cell receptor / MHC protein complex (mouse)[2CKB] 263—265
TATA-box binding protein (yeast) [1YTF] 330
TCR see “T-cell receptor”
TE33 (mouse) [1TET] 86
TE33 (mouse) [1TET], antigen-binding site 245
TE33 (mouse) [1TET], L3 canonical structure 242
Tertiary structure 70
Tetracycline repressor (Escherichia coli) [2TCT] 315
Tetrahydrodipicolinate-N-succinyltransferase (Mycobacterium bovis) [1TDT] 321
Thaumatin (African berry) [1THW] 320
Thermostability 19 23 37
Thioredoxin (Anabaena sp) [1THX] 92
Thrombin (human) + hirulog-3 [1ABI] 208
TIM barrel 70 152 173
TIM barrel, packing of interior 154ff
TIM barrel, topology 154
Timothy grass pollen allergen [1WHO] 81 162
Tobacco mosaic virus [2TMV] 109—110
Tomato bushy stunt virus [2TBV] 101—102
Transcription factor Skn-1 (Caenorhabditis elegans) [1SKN] 120
Transfer RNA, Phe (yeast) 62
Transthyretin (human) [1ETA] 144
Triosephosphate isomerase (Trypansoma brucei) [6TIM] 96
Triosephosphate isomerase (yeast) [7TIM] 330
Troponin C (chicken) [4TNC] 311
Trp repressor (Escherichia coli) [3WRP] 311
Trypsin (and BPTI) [1TPA] 108
Turns see “Loops”
Twilight Zone 95
Ubiquitin (human) [1UBQ] 324
Uniform resource locator (URL) 44
Uteroglobin (rabbit) [1UTG] 80
Van der Waals forces 30
Vk L3 loops, canonical structures 242—243
Water 110
Wheat germ agglutinin [9WGA] 158
World Wide Web 16 43ff
World Wide Web archives 46
World Wide Web protein classification 43
World Wide Web tools 48
World Wide Web useful sites see appendix 2
X-ray crystallography 1 37ff 42 110
Zinc-finger 103
Zinc-finger Zif268 (mouse) [1AAY] 25
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