I-40 Index
Prokaryotes, 3–6, 4F. See also specific
organisms
chain elongation, 1379–1388
chain initiation, 1373–1376
chain termination, 1391–1392, 1392F
citric acid cycle, 789, 814–815
DNA replication, 1173, 1190–1201
DNA size, 94T
eukaryotic protein production in, 118
evolution, 13F, 34
fMet, 1373–1374
genome sequencing, 176
introns of, 1316
mismatch repair, 1220
mRNA posttranscriptional
modification, 1302
nucleotide excision repair, 1217
ribosomes of, 1369–1371
transcription control, 1283–1301
transformation by DNA, 85–86
translational initiation, 1375–1376
transposons of, 1236–1244
Prokaryotic gene expression:
mRNA lifetime, 101
RNAP, 1265
transcription, 96–97, 101, 1269
translation, 101
Proliferating cell nuclear antigen, see PCNA
Proline:
amino group, 67
biosynthesis, 1071
degradation, 1034
genetic codes for, 100T, 1343T
helix/ sheet propensity, 302T
low helix propensity, 304
in native unfolded proteins, 283
as nonessential amino acid, 1065T
in PEST proteins, 1413
Ramachandran diagram, 225
side chains, 70, 264T
specific rotation, 74
structure and general properties, 68T
Proline racemase, 516
Prolyl 3-hydroxylase, 1405
Prolyl 4-hydroxylase, 1405
Prolyl hydroxylase, 236
Promoters, 97, 571, 1266–1267, 1284
Pronucleus, 121, 121F
Proofreading, 1201
DNA chain, 1177
of synthesized proteins, 1390–1391
of tRNA, 1355–1358
1, 2-Propanediol, 1018
Propeller, 433
Propeptides, 1403–1404
Prophase, 20F, 21F
Prophospholipase A
2
, 538
Propionaldehyde, 1018
Propionic acid, 32T
Propionyl-CoA carboxylase, 952–953
Propionyl-CoA carboxylase reaction, 953F
Proportional counting, 572
Propranolol, 680
Proproteins, 1403–1404
pro-R, 77, 77F
pro-S, 77, 77F
Prostacyclins, 993, 995–1000
Prostacyclin I
2
(PGI
2
), 997, 998
Prostacyclin receptors, 689
Prostacyclin synthase, 998
Prostaglandins (PGs), 971, 993–995, 994F,
995F, 997–1000
Prostaglandin endoperoxide synthase, 997
Prostaglandin H
2
synthase, 406, 997
Prostaglandin receptors, 689
Prostanoic acid, 993–994
Prostate cancer, 1236
Prosthetic group, 473
Proteases, 101, 131, 1419–1420
Protease A, 525T
Protease B, 525T
20S Proteasome, 1411F, 1415, 1415F
26S Proteasome, 1411–1412, 1414
Proteasomes, in ubiquination, 1411–1412
Protection of telomeres 1 (POT1), 1213
Protective antigen (PA), anthrax, 715
Proteins, 15. See also related topics, e.g.:
Amino acids
amino acid derivatives in, 78–79, 80F
amino acids of, 67–73, 68T–69T
beta structures, 229–232
in biological processes, 67
and buffers, 48
chemical evolution of, 189–192, 191F
and chemical synthesis of polypeptides,
206–209
in chromatin, 8
conformational diseases, 309–316
crystal, 122
cyclic symmetry, 268, 268F
denatured, 57
design of, 305–306
dihedral symmetry, 268, 268F
essential amino acids in, 1064
evolution of, 192–196, 196F, 316–318
fibrous, see Fibrous proteins
functional groups of, 43
fusion, 118
globular, see Globular proteins
helical structures, 225–229
helical symmetry, 269, 269F
homologous, 189–192
icosahedral symmetry, 268, 268F
from inclusion bodies, 117
and molecular cloning, 117–121
motifs, 249–251
number of, 70
octahedral (cubic) symmetry, 268, 268F
one gene–one polypeptide maxim, 26
organization of, 17F, 163–164, 281–282, 281F
physical constants of, 153T
polyproteins, 1404
posttranslational modification and
degradation of, 101
primary structure, see Protein sequencing
pseudosymmetric, 268
for purification, 130
quaternary structure, 266–271, 267F
roles of, 163
secondary structure, 221–233, 302–304
solubilities of, 133–135
structures of, 230–233
subunit interactions, 267
supersecondary structures, 249–251
symmetry, 267–270
tertiary structure, 245–256, 304–305
tetrahedral symmetry, 268, 268F
titration curves, 72, 72F
in translation, 98–101
ubiquitin attachment to, 1410F
1
-Proteinase inhibitor, 533
Proteinase K, 1383
Protein assays, 131–132
Protein C, 1317
Protein-conducting channel (PCC), 424, 426
Protein crystals, 134F
Protein Data Bank (PDB), 256–257, 256T, 259
Protein degradation, 1408–1411. See also
Polyubiquitin; Ubiquitin
Protein denaturation, 57, 221, 262, 265–266
Protein disulfide isomerase, see PDI
Protein dynamics, 306–309
Protein families (Pfam), 256T, 258
Protein folding, 537
accessory proteins, 290–302
determinants, 281–284
endoplasmic reticulum, 427–428
GroEL/ES system, 294–302
hierarchical nature of, 289
landscape theory of, 287–289, 288F
pathways, 284–290
peptidyl prolyl cis-trans isomerases, 292
protein disulfide isomerases, 280, 290–292,
290F, 291F
and pulsed H/D exchange, 285–286
and renaturation, 278–281
Protein folding funnels, 287–289, 288F
Protein folding problem, 278
Protein G, 282
Protein GB1, 282, 282F
Protein growth factors, 671
Protein Information Resource (PIR), 195T
Protein Interfaces, Surfaces and Assemblies
(PISA), 256T
Protein isolation, 129–133
Protein kinases, 670, 973, 975
Protein kinase A (PKA), 651–654
Protein kinase B (PKB), 734, 737F
Protein kinase C (PKC), 660, 698, 713, 727,
730–732
Protein metabolism, 561F
Protein phosphatases, 721–725
Protein phosphatase-2A, 699, 723F
Protein purification, 129–156
chromatographic separations, 135–146
electrophoresis, 146–152
general strategy, 132–133
and protein isolation, 129–133
and protein solubilities, 133–135
ultracentrifugation, 152–156
Protein renaturation, 278–281
Protein Research Foundation (PRF), 195T
Protein sequence databanks, 195T
Protein sequencing, 164–165
C-terminus identification, 165–168
disulfide bond cleavage, 168–169
disulfide bond position assignment, 172
Edman degradation, 165, 167F, 171,
172, 174
end group analysis, 165–168
N-terminus identification, 165
nucleic acid sequencing contrasted,
184–185
peptide characterization and sequencing
by mass spectrometry, 172–174, 172F
peptide cleavage reactions, 169–171
peptide fragments, ordering, 171
peptide fragments, separation and purifi-
cation of, 171
peptide mapping, 174–175, 175F
separation, purification, and characteriza-
tion of polypeptide chains, 169
sequence alignment, 194–203
sequence databases, 194–195
sequence determination, 171, 171F
Protein Ser/Thr phosphatases, 722
Protein solubilization, 130
Protein splicing, 1405–1408
Protein stability, 130–131
and denaturation, 265–266
and disulfide bonds, 264–265
electrostatic forces, 259–261
hydrogen bonding, 261–262
hydrophobic forces, 262–264
thermostable proteins, 266
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