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Lesk A.M. — Introduction to Protein Architecture
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).


Язык: en

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

Операции: Положить на полку | Скопировать ссылку для форума | Скопировать ID
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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 $\beta$-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 $A_{2}$ (cow) [1BP2]      81
Phospholipase $A_{2}$ (Taiwan cobra) [1POA]      312
Phospholipase $A_{2}$ (western diamondback rattlesnake) [1PP2]      314
Phosphotyrosine protein phosphatase (cow) [1PHR]      331
Photoactive yellow protein (Ectothiorhodospira halophila), $\pi$-helix [2PHY]      65—66
Photosynthetic reaction centre      1
Photosynthetic reaction centre (Rhodopseudomonas viridis) [1PRC]      2 4—9
Phycocyanin (Mastigocladus laminosus), $\alpha$-chain      202
Phycocyanin (Mastigocladus laminosus), $\alpha$-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), $S\rightarrowR$ transition      291
Serum response factor, core fragment (human) [1SRS]      329
Shear number of $\beta$-barrel      154 213
Sheet      see “$\beta$-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
1 2
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