ライフサイエンスコーパス: tryptophan residue

1 unaffected by the introduction of the bulky tryptophan residue.

2 complex via an acidic motif with a conserved tryptophan residue.

3 holog involving a strictly conserved surface tryptophan residue.

4 exible, acidic sequences containing a single tryptophan residue.

5 ther peroxidases by the presence of a distal tryptophan residue.

6 nt, and the native packing around the single tryptophan residue.

7 cross-linking of that side chain to a second tryptophan residue.

8 x anchored to the liposome by an interfacial tryptophan residue.

9 cross-linking of that side chain to a second tryptophan residue.

10 odynamic and kinetic description of a buried tryptophan residue.

11 induced by changing the position of a nearby tryptophan residue.

12 in revealed a rather dynamic picture for the tryptophan residue.

13 ain, the DNA-binding domain, and a conserved tryptophan residue.

14 competing reaction pathways of (1)O(2) with tryptophan residues.

15 homodimer structure containing 26 structural tryptophan residues.

16 ockets building an aromatic tetrade with two tryptophan residues.

17 photoinduced electron transfer reaction from tryptophan residues.

18 fluorescence in proteins is dominated by the tryptophan residues.

19 W and F17W reveal molecular details of these tryptophan residues.

20 translational modification of two endogenous tryptophan residues.

21 on byproduct arising from the indole ring of tryptophan residues.

22 rogen bonds and hydrophobic contacts between tryptophan residues.

23 cture and a change in the environment of the tryptophan residues.

24 on of helices and structure formation around tryptophan residues.

25 alpha-Synuclein has four tyrosine and no tryptophan residues.

26 IdeR contains two tryptophan residues.

27 e major products were mono- and dioxygenated tryptophan residues.

28 photolysis, and oxidation of methionine and tryptophan residues.

29 sthetic molecules with the channel-anchoring tryptophan residues.

30 nly due to energy migration between adjacent tryptophan residues.

31 ght peripheral alpha-helices containing four tryptophan residues.

32 ificantly affected by the replacement of the tryptophan residues.

33 d by a double cation-pi interaction with two tryptophan residues.

34 lly those alpha-helix sections which contain tryptophan residues.

35 ored via the anodic reaction of tyrosine and tryptophan residues.

36 tertiary structure and more solvent-exposed tryptophan residues.

37 in oxidative modifications to methionine and tryptophan residues.

38 ter the conformation of MDM2 surrounding the tryptophan residues.

39 tween a flavin cofactor (FAD) and a triad of tryptophan residues.

40 form distinct clusters around two conserved tryptophan residues.

41 rms reveals differences in key cysteines and tryptophan residues.

42 es with the average solvent exposure time of tryptophan residues.

43 structural changes leading to an exposure of tryptophan residues.

44 We defined that substitution of tryptophan residue 128 in the CsA-binding site of CypB w

45 n the centers of the indole rings of the two-tryptophan residues, 2 and 4, and the epsilon-methylated

46 nt FMDVs containing substitutions at 3D(pol) tryptophan residue 237 were genetically stable and displ

47 We previously identified E2 tryptophan residue 420 (W420) as an essential CD81-bindi

48 ates the role of a highly conserved residue, tryptophan residue 420, of the viral glycoprotein E2 in

49 ylation (C-mannosylation) were identified at tryptophan residues 43 and 61.

50 an number reduction with substitution of all tryptophan residues ablating dimerization and self-renew

51 toplasmic loops, the extracellular plug, all tryptophan residues, an ordered cholesterol molecule and

52 escribed, hydrophobic interactions between a tryptophan residue and the beta-galactoside alpha face a

53 the protein villin, which contains a single tryptophan residue and was engineered to contain a cyste

54 a relatively greater burial of cysteine and tryptophan residues and are more compact as compared to

55 ng process, C-mannoses orient the underlying tryptophan residues and facilitate the formation of the

56 formation occludes hydrophobic surfaces and tryptophan residues and leads to a partial loss of alpha

57 head domain (subfragment 1 or S1) has seven tryptophan residues and nucleotide-induced fluorescence

58 e fluorescent signal completely to the three tryptophan residues and observation of the presence of o

59 iposomes, increased solvent exposure of MPER tryptophan residues and stable docking of 2F5 and 4E10 m

60 stabilizing the local positioning of the two tryptophan residues and the conformation of adjacent cha

61 ict specificity of the enzyme for lysine and tryptophan residues and the dependence of an eight-amino

62 ied movement of the peptide groove obscuring tryptophan residue, and consequent opening up of the bin

63 ich results in the replacement of R64 with a tryptophan residue, and we demonstrate this substitution

64 , contains two phenylalanine residues, three tryptophan residues, and two proline residues.

65 Experiments demonstrate that tryptophan residues are also responsible for the low lev

66 the 100 ms time scale, indicating that these tryptophan residues are buried only during the late stag

67 Five tryptophan residues are dispersed in the primase of bact

68 terations in the excited state properties of tryptophan residues are easily visualized using the phas

69 tion and that solvent-exposed methionine and tryptophan residues are likely initial targets of oxidat

70 P (pH-Low Insertion Peptide) variants, where tryptophan residues are located near the N terminus, nea

71 oxidation product, where both methionine and tryptophan residues are oxidized, yielding a deactivated

72 ne side chains, each one located between two tryptophan residues, are critical to insoluble and solub

73 f CheA that had been engineered to include a tryptophan residue as a fluorescent reporter group at th

74 Using intrinsic flavin cofactor and tryptophan residue as the local optical probes with two

75 hotoreduction process, which involves nearby tryptophan residues as electron donors.

76 ssion of proteins bearing solvent accessible tryptophan residues as reactive handles for modification

77 opulations tended to recognize peptides with tryptophan residues as TCR contacts.

78 ange in casein hydrophobicity by exposure of tryptophan residues, as confirmed by spectroscopic metho

79 f several proteins with different numbers of tryptophan residues assembled on the surfaces of quartz

80 The data suggest how BNAbs may perturb tryptophan residue-associated viral fusion involving the

81 OmpA mutants with a single tryptophan residue at a nonnative position 170 (Trp-170)

82 However, mutation of the tryptophan residue at amino acid 139 significantly impai

83 The FZD2 mutation (c.1644G>A) changes a tryptophan residue at amino acid 548 to a premature stop

84 which an arginine residue is replaced with a tryptophan residue at codon 62 (RPS19R62W).

85 ble proteins-maquettes-that contain a single tryptophan residue at different distances from a covalen

86 ip by making MDE mutants containing a single tryptophan residue at each of the seven positions found

87 Thus, a tryptophan residue at position 12 of the peptidyl-tRNA T

88 Other spectral changes are observed for a tryptophan residue at position 15, and these modificatio

89 identified two regions of VirB6, a conserved tryptophan residue at position 197 and the extreme C-ter

90 to create hydrophobic interactions with the tryptophan residue at position 316 and with other topolo

91 sigma(32) is at the homologous position of a tryptophan residue at position 433 of the main sigma fac

92 ky aromatic substituents at position 5 and a tryptophan residue at position N-3 of the rhodanine ring

93 Mutants, containing a single tryptophan residue at the native positions 7, 15, 57, 10

94 ) obtained from tuna heart, which contains a tryptophan residue at the site occupied by His33 in hors

95 n in the light sleeper peptide suggests that tryptophan residues at N- and C-termini may be preferent

96 Tryptophan residues at position 5 in each finger provide

97 Human PNP is a homotrimer containing three tryptophan residues at positions 16, 94, and 178, all re

98 a homotrimer, containing three nonconserved tryptophan residues at positions 16, 94, and 178, all re

99 micidin A have been synthesized in which the tryptophan residues at positions 9, 11, 13, and 15 are s

100 The results indicate that tryptophan residues at the dimer interface engage in pho

101 During cofactor formation, the two tryptophan residues become covalently linked, and two ca

102 quantify the extent to which an intervening tryptophan residue can facilitate electron transfer betw

103 Chains of redox-active tyrosine and tryptophan residues can transport potentially damaging o

104 The damaged tryptophan residues cause large fluctuations in the Tyr-

105 elix in the peptide, containing an important tryptophan residue, contacts S100B.

106 y transfer analysis of mutants with specific tryptophan residues converted to phenylalanine residues

107 We have further identified two tryptophan residues critical for LITE-1 function.

108 Tryptophan residues critical to function are frequently

109 n drug response, suggesting that the bulkier tryptophan residues directly block stimulator binding.

110 The enzyme contains five tryptophan residues distributed evenly over all four fun

111 ystallization studies confirm that these two tryptophan residues do not alter the structure of HC/B o

112 The replacement of the tryptophan residues does not have a significant effect o

113 cifically, polymorphisms at highly conserved tryptophan residues (e.g., Trp-57 and Trp-183) and immun

114 structural data for particular tyrosine and tryptophan residues, enabled assignments based on predic

115 uorescence resonance energy transfer between tryptophan residues engineered into gamma and trinitroph

116 This oxidized tryptophan residue exhibited a distinct absorption band

117 ot be subunit-delimited, and (v) the mutated tryptophan residues experience energy changes that occur

118 sorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as

119 kinetics, helix formation and structure near tryptophan residues for a variety of proteins.

120 to Arabidopsis thaliana UVR8, has conserved tryptophan residues for UV-B photoreception, monomerizes

121 tational studies have identified two crucial tryptophan residues for UV-B responses in AtUVR8.

122 In the structure, four tryptophan residues form a tight hydrophobic cage encasi

123 Interestingly, a ring of tryptophan residues forms the narrowest constriction in

124 espond to the extraction of the two pairs of tryptophan residues from the membrane.

125 Dd) myosin II constructs containing a single tryptophan residue have revealed detailed information re

126 he increased fluorescence, the mechanism and tryptophan residues have not been identified.

127 ownstream of the Eh-1 domain that contains a tryptophan residue implicated in protein-protein interac

128 or ZM241385 in restricting the movement of a tryptophan residue important in the activation mechanism

129 d presence of external (phenol) or internal (tryptophan residue in an I100W variant) substrates under

130 A tryptophan residue in both AADs is required for ATR acti

131 Dps proteins contain a conserved tryptophan residue in close proximity to the iron-bindin

132 Filling this cavity with a histidine or tryptophan residue in Env with a natural serine residue

133 more, we found that the conserved and single tryptophan residue in PET, Trp 536, moves to a more hydr

134 s the P(I/L)W subfamily, that have evolved a tryptophan residue in place of the (D/E) in the second c

135 We have searched for a tryptophan residue in RAG1 that would be the functional

136 rvation to lie at a position equivalent to a tryptophan residue in rhodopsin at the 3,4,5 helix inter

137 Mutation of a single tryptophan residue in the alpha3b helix of DH reduces bi

138 interaction between the natural ligand and a tryptophan residue in the aromatic box, and does this in

139 f oxidation was identified to be a conserved tryptophan residue in the heavy chain complementarity de

140 We revealed that a conserved tryptophan residue in the human eIF3j N-terminal acidic

141 A conserved tryptophan residue in the loop was identified as critica

142 A conserved TxPsi motif adjacent the tryptophan residue in the loop was required for pre-mRNA

143 Mutation of the subfamily-defining tryptophan residue in the MFT to match the MCF consensus

144 henylalanine to form an enzyme with a single tryptophan residue in the mobile loop.

145 A single tryptophan residue in the N-terminal 17-residue linker m

146 ins, we found that mutation of the invariant tryptophan residue in the PH domain did not impair Delta

147 Mutation of a conserved tryptophan residue in the RAG-2 PHD finger abolished bin

148 interface comprising the side chains of four tryptophan residues in a co-planar linear arrangement.

149 ive conditions consistent with burial of the tryptophan residues in an apolar environment.

150 utilizing brominated lipids reveal that the tryptophan residues in both mutants are essentially equi

151 lipid peroxidation, and protect lipoprotein tryptophan residues in human LDL.

152 a pH-dependent change in the environment of tryptophan residues in imiglucerase that is absent in N3

153 nd kynurenin formation from the oxidation of tryptophan residues in LDL.

154 There are four tryptophan residues in mADA and all are located more tha

155 The six conserved tryptophan residues in NP can be used as an intrinsic pr

156 r nanostructures to increase the emission of tryptophan residues in proteins.

157 The engineered tryptophan residues in the beta-barrel and the N-termina

158 members reveals the presence of one or more tryptophan residues in the carbohydrate-recognition doma

159 r deleterious auto-oxidation of tyrosine and tryptophan residues in the enzyme's framework.

160 f D1/D2 CD4, which contains two of the three tryptophan residues in the gp120-binding domain.

161 Mutation of two critical tryptophan residues in the hydrophobic peptide disrupted

162 isoalloxazine ring is sandwiched between two tryptophan residues in the interface of the dimeric prot

163 thetaiotaomicron (termed ppBat) exhibits two tryptophan residues in the interface which enable specif

164 uncation of PDGFRalpha between two conserved tryptophan residues in the juxtamembrane (JM) domain is

165 ed the contributions of the three individual tryptophan residues in the N-lobe (Trp8, Trp128, and Trp

166 Excitation of FK1 domain native tryptophan residues in the presence of bound ligand resu

167 to monitor the change in fluorescence of the tryptophan residues in the protein upon binding to an NP

168 and taking advantage of the high content of tryptophan residues in the sequence of PB1-F2 (5/90 aa),

169 DPY19 family that transfer alpha-mannoses to tryptophan residues in the sequence WX (2)WX (2)C, which

170 VE-cadherin and demonstrated that conserved tryptophan residues in this sequence are required for VE

171 erferometry, we identified several conserved tryptophan residues in TTP that serve as major sites of

172 For mAb C, all tryptophan residues including one in the heavy chain CDR

173 with no significant oxidation found on other tryptophan residues including those in close proximity t

174 Fluorescence quenching of inserted tryptophan residues indicated the entry of anions into t

175 We incorporated in turn a tryptophan residue into each of the three helices of the

176 densely packed native core, which brings the tryptophan residues into close contact with intramolecul

177 ing degrees of change in the fluorescence of tryptophan residues introduced at specific sites within

178 formed by an induced fit in which one of the tryptophan residues involved in cap binding flips throug

179 Furthermore, three of the nine tryptophan residues involved in the different ligand-bas

180 lly different flap structure, in which a key tryptophan residue is displaced, and the aromatic group

181 These results indicate that (i) each rim tryptophan residue is involved in binding a PC molecule

182 tivation experiments, which suggest that the tryptophan residue is reverse prenylated by CymD prior t

183 neered a GAC protein (GAC(F327W)) in which a tryptophan residue is substituted for phenylalanine in a

184 The fluorescence from native actin tryptophan residues is not significantly perturbed on bi

185 in comprising three evolutionarily conserved tryptophan residues known as the Trp triad.

186 rkably, switching the stereochemistry of the tryptophan residue (l to d) stabilizes the dimerizer*Exd

187 A reduction in the number of tryptophan residues leads initially to a gradual reducti

188 the flavin adenine dinucleotide cofactor and tryptophan residues leads to the formation of a spin-cor

189 ole-hopping mechanism is proposed in which a tryptophan residue located between the hemes is reversib

190 The W420 tryptophan residue located closest to the FAD-dCRY inter

191 study, we analyzed the roles of tyrosine and tryptophan residues located within TM1-6 with a goal of

192 In particular, the single tryptophan residue, located near the end of helix IV, an

193 tronic coupling values, tunneling over three tryptophan residues may become competitive in some cases

194 onous fluorescence spectra revealed that the tryptophan residue microenvironment of betaLG was affect

195 ally occurring Vpu proteins, we found that a tryptophan residue near the Vpu C terminus is particular

196 lication and identify conserved arginine and tryptophan residues near its C-terminus that are needed

197 ic amino acids and nucleic acids (AAA + NA), tryptophan residues, nicotinamide adenine dinucleotide (

198 Tryptophan residue number 38 of chNHE1 (W38) in the extr

199 ture previously reported for IL-16 reveals a tryptophan residue obscuring the recognition groove.

200 ifications on four tyrosine residues and one tryptophan residue of hemopexin.

201 emission spectra revealed that the (single) tryptophan residues of the individual domains underwent

202 Highly conserved tryptophan residues of the MbtH-like domain critically c

203 d a shift in the fluorescence maximum of the tryptophan residues of the peptide.

204 e we report that mutation of the 2 conserved tryptophan residues of the WW-like domain has opposing e

205 Tryptophan residues often are found at the lipid-aqueous

206 phate group is positioned to interact with a tryptophan residue on the neighboring strand.

207 modification of free cysteine, tyrosine, and tryptophan residues on LPO.

208 dence for lipid-protein interactions for the tryptophan residue oriented toward the interior of the b

209 e protein A (OmpA), and focus on interfacial tryptophan residues oriented toward the lipid bilayer (t

210 Conserved tryptophan residues outside of the IBB are required for

211 mane fluorophore in Loop V-VI is quenched by tryptophan residues placed at 148 or 298.

212 These results suggest that this tryptophan residue plays a key role in masking the NES o

213 Its natural substrate is a monohydroxylated tryptophan residue present in a 119-kDa precursor protei

214 The four tryptophan residues present in the enzyme have been chan

215 ligand-induced shifts in the fluorescence of tryptophan residues present in the scaffold proteins of

216 Glycosylation of tryptophan residues represents a new lens protein modifi

217 d sufficient for interaction with Sox2, with tryptophan residues required.

218 ctroscopy, predicated on the manner in which tryptophan residues reside and move within protein micro

219 To identify the tryptophan residues responsible for the increased fluore

220 sequence or substitution of key arginine or tryptophan residues results in loss of antiviral activit

221 N-terminal half only, or mutation of the key tryptophan residues results in the severe leaky scanning

222 oscopy on W322F, a mutant of the neighboring tryptophan residue, revealed a decrease of the tyrosyl r

223 an average tilt of 24 degrees, with the five tryptophan residues sampling different environments insi

224 Phi value analyses (of both tryptophan residues) show Phi approximately 1 for both t

225 ptide backbone and affects the position of a tryptophan residue shown in other WW domains to play a k

226 its to bind YxxPhi cargo motifs with its two tryptophan residues sitting in compatible pockets.

227 odified phospholipids of the fluorescence of tryptophan residues substituted into cytochrome P450 2C2

228 t shift register with respect to a conserved tryptophan residue, supporting a "spring-loading" mechan

229 onist binding site by positioning a critical tryptophan residue that directly contacts the ligand.

230 cated in the dimer interface and a conserved tryptophan residue that engages in hydrogen bonding or a

231 the highly conserved glycine, tyrosine, and tryptophan residues that define the kelch repeat sequenc

232 for a crucial role of a cluster of conserved tryptophan residues that expose a pH-sensitive loop of F

233 The MPER has an unusually high percentage of tryptophan residues that likely contribute to the membra

234 d by post-translational modifications of two tryptophan residues that result in the incorporation of

235 tulates a set of interdigitated arginine and tryptophan residues that stabilize a distinctive beta-st

236 scence intensity and emission maximum of the tryptophan residues that strongly depended on protein co

237 rate proteins, each containing only a single tryptophan residue, that the rate constant for singlet o

238 ined by a small motif consisting of adjacent tryptophan residues (the W(202)W(203) motif).

239 stitution of a fully conserved and essential tryptophan residue to glycine, and, as expected, this pr

240 depends not only on the accessibility of the tryptophan residue to oxygen, but also on factors that c

241 were confirmed with a major contribution of tryptophan residues to fluorescence quenching.

242 or the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylqui

243 iheme enzyme that oxidizes two protein-bound tryptophan residues to generate a catalytic tryptophan t

244 and results in the coupling of tyrosine and tryptophan residues to phenylene diamine and anisidine d

245 lity of peptides containing N- or C-terminal tryptophan residues to quench bimane fluorescence was me

246 tertiary structure, and partial exposure of tryptophan residues to solution being approximately conc

247 uorescence energy transfer from the enzyme's tryptophan residues to the probe.

248 examined the effects of mutating individual tryptophan residues to tyrosine, alanine, or phenylalani

249 depends on the presence of a solvent-exposed tryptophan residue (Trp-164).

250 tics, we have expressed a variant in which a tryptophan residue (Trp-38) in the middle of the active

251 -37) that acts as a selectivity filter and a tryptophan residue (Trp-41) that acts as a channel gate.

252 The solvent-exposed MPER tryptophan residue (Trp-680) was immunodominant, focusin

253 rt, we show that an evolutionarily conserved tryptophan residue (Trp-73) of Y14 is critical for its b

254 ligand, which accepts a H-bond from a nearby tryptophan residue, Trp-188.

255 e (C6PS) binding pocket flanked by a pair of tryptophan residues, Trp(2063) and Trp(2064).

256 Two tryptophan residues, Trp106 and Trp113, on the surface o

257 A tryptophan residue (Trp141) from the neighbouring subuni

258 Spectral contributions of two tryptophan residues, Trp17 and Trp120, present in the wi

259 ioferritin (BFR), due to the presence of two tryptophan residues (Trp35 and Trp133) in each of the 24

260 Two tryptophan residues (Trp47 in the two-turn helix B and T

261 proposed view that, during activation, this tryptophan residue undergoes a rotameric transition that

262 electron transfer down a conserved chain of tryptophan residues underlies biological responses follo

263 els of HOCl-derived oxidized and chlorinated tryptophan residues W(28) and W(192) are significantly e

264 affect the catalytic activity, including one tryptophan residue W127 that likely acts through regulat

265 Of those, a tryptophan residue (W242) at an alpha-helix of CyaA make

266 nce signal from Y162W by removing two native tryptophan residues (W270A/W284A).

267 Mutation of the dCRY tryptophan residue W342, more distant from the FAD inter

268 y undergo an ultrafast reduction by a nearby tryptophan residue W400.

269 Notably, a conserved tryptophan residue (W453) that constitutes a key structu

270 ously, we have demonstrated that a conserved tryptophan residue (W512) is a major contributor to nucl

271 rescence energy transfer studies between the tryptophan residue W92 and the acceptor, located at the

272 ence studies using a Cdc42 mutant in which a tryptophan residue was introduced at position 32 of Swit

273 structural contacts during folding, a unique tryptophan residue was introduced at seven partially bur

274 ne that uses the intrinsic fluorescence of a tryptophan residue, we have also measured the second-ord

275 The site-specific oxidation of tryptophan residues were confirmed by liquid chromatogra

276 The two tryptophan residues were found to pack against the lysin

277 Two tryptophan residues were incorporated on one face of a b

278 mutated to tryptophan, and the three native tryptophan residues were mutated to phenylalanine to for

279 early all methionine, cysteine, and (likely) tryptophan residues were oxidized.

280 of different aromatic interactions, selected tryptophan residues were substituted with Tyr to get thr

281 Selected tryptophan residues were substituted with Val to test th

282 Endogenous tryptophan residues were used as donors, the substrate a

283 utants, each containing the single remaining tryptophan residue, were produced.

284 y the level of beta oxidation of the priming tryptophan residue, which is oxidized in the cyclomarin

285 ormed of a pathway of conserved tyrosine and tryptophan residues, which can protect the protein activ

286 Both glutamine and tryptophan residues, which occur frequently in the metal

287 e mutations at six positions, including four tryptophan residues, which result in mutant envelope gly

288 nce receptors Tar and Tsr, TM2 is flanked by tryptophan residues, which should localize preferentiall

289 nimal cryptochromes, feature a chain of four tryptophan residues, while other members of the family c

290 either complete or individual replacement of tryptophan residues with 5-fluorotryptophan ((5F)W).

291 nal residues, including one or two conserved tryptophan residues, with a leucine-rich nuclear export

292 vironment, medin is nitrated at tyrosine and tryptophan residues, with resultant effects on morpholog

293 Moreover, the authors identified a tryptophan residue within a specific monoclonal FLC that

294 apoA-I mutants containing a single reporter tryptophan residue within each of its 22 amino acid amph

295 nally heterogeneous type II chaperonins, the tryptophan residue within the alpha subunit was used as

296 electrophysiological responses, while other tryptophan residues within electron transfer distance to

297 gh the posttranslational modification of two tryptophan residues within MADH, during which the indole

298 ow that substitution of two highly conserved tryptophan residues within the juxtamembrane domain (JMD

299 urther suggest that direct photooxidation of tryptophan residues within the protein structure are sig

300 ly derived from the interaction of iron with tryptophan residues within the subunit dimer.