ライフサイエンスコーパス: Trp residue

1 mouse C5aRs with a residue exchange of this Trp residue.

2 linked to the N-1 atom of the indole ring of Trp residue.

3 en bond, but preserves other properties of a Trp residue.

4 Each of its two ZFs has a Trp residue.

5 t of the spectral signal from the introduced Trp residue.

6 s I and II are relatively far away from this Trp residue.

7 with the methyl group pointed toward another Trp residue.

8 t the C2 position of the indole ring of each Trp residue.

9 n which L722(PsaA) was replaced with a bulky Trp residue.

10 to native PNP, suggesting a solvent-exposed Trp residue.

11 Ribonuclease Sa (RNase Sa) contains no Trp residues.

12 se is influenced to different extents by all Trp residues.

13 elocity, and intrinsic fluorescence of the 2 Trp residues.

14 s residues 86-601 (PutA86-601) and only four Trp residues.

15 cL) and Escherichia coli (EcMscL) contain no Trp residues.

16 ng of the fluorescent label bimane by nearby Trp residues.

17 nt proteins, each of which lacks one or more Trp residues.

18 nt domain motion was detected for any of the Trp residues.

19 Ca2+-binding loops were replaced by reporter Trp residues.

20 s were assigned by mutagenesis of the native Trp residues.

21 little change in the microenvironment of the Trp residues.

22 iving force for the high conservation of the Trp residues.

23 clease Sa (RNase Sa) contains no tryptophan (Trp) residues.

24 per monomer to hydrophobic (two Phe and one Trp) residues.

25 exibility in the vicinity of the tryptophan (Trp) residues.

26 an indole nitrogen protons shows that buried Trp residues 123, 111, and 108 lose tight packing and be

27 the presence of a 162-Da substituent in each Trp residue; 2) the presence of abundant fragments of m/

28 residues are in the aqueous phase, all three Trp residues adopt interfacial positions, and several hy

29 The conserved Trp residues, after which this domain was named, were re

30 Additionally, a mutant lacking all three Trp residues allows assignment of the fluorescent signal

31 There are three Trp residues (alpha14, beta15, and beta37) in Hb A for e

32 t side chains, particularly those of Phe and Trp residues, also confirm different local interactions

33 ntramolecular distances between an intrinsic Trp residue and BODIPY-labeled S16Meso depend on the lev

34 ational dynamics through interactions with a Trp residue and fields originating on charge sites.

35 The environment of each Trp residue and the pyridoxyl phosphate in both an equil

36 When Trp residues and acrylodan were used as donor-acceptor p

37 indicated a decrease in the mobility of the Trp residues and an increase in the flexibility of fluor

38 Trp residues and basic residues are abundant at the memb

39 This activity requires the Trp residues and is independent of CD36-binding sequence

40 Three conserved Trp residues and one non-conserved Tyr residue, shown pr

41 epresent direct burial of one or both of the Trp residues and parts of the G- and H-helices.

42 isotropy measurements were made of the three Trp residues and pyridoxal 5'-phosphate, attached covale

43 e in the anchoring interaction between these Trp residues and the DMPC interfacial region.

44 tude of a CD exciton couplet (due to the two Trp residues) and the chemical shifts of a Trp Hepsilon3

45 )]URP and [Tpi(4)]URP, also suggest that the Trp residue, and more specifically the indole ring, is n

46 mation had been predicted for the engineered Trp residue, and the lowered oxygen affinity had been at

47 was completely symmetrical, rich in Arg and Trp residues, and able to adopt a native RTD-1-like stru

48 Thr, Asn, Gln, Asp, Glu, His, Arg, Lys, and Trp) residues, and intervening regions that consist of b

49 etely quenched or two highly quenched enzyme Trp residues approximately 10 and approximately 17 A, re

50 f CerSs which contain a Hox-like domain, the Trp residues are asymmetrically distributed throughout t

51 These observations suggested that the two Trp residues are buried and constrained in a hydrophobic

52 FRET is observed despite the fact that these Trp residues are close enough for significant FRET to oc

53 actions between similarly positioned His and Trp residues are essential for gating and the girdle-lik

54 f HXXXW, and, for both proteins, the His and Trp residues are important for channel function.

55 Therefore, both Trp residues are involved in the phenomenon.

56 Since the Trp residues are located exclusively in the beta-roll cy

57 These Trp residues are located in important regions of the Hb

58 The Trp residues are located in intrinsically disordered reg

59 e quenching by acrylamide indicates that the Trp residues are not considerably exposed to the solvent

60 When these Trp residues are replaced with Gly in either recombinant

61 the unfolding free energy of LacY and employ Trp residues as site-specific thermodynamic probes.

62 Our work also highlights the role of Trp residues as tunable redox-active cofactors for enzym

63 es for a lasso peptide with an unprecedented Trp residue at its N-terminus, a peptide we have named f

64 Of particular importance are the Trp residue at position 29 and the 3 arginines in the re

65 ytoplasmic side of the membrane close to the Trp residue at position 87, with binding to one of these

66 of b12 is crucially dependent not only on a Trp residue at the apex of the H3 loop but also on a num

67 ence measurements of the membrane depth of a Trp residue at the center of a hydrophobic sequence.

68 e membrane by fluorescence, each contained a Trp residue at the center of the sequence.

69 onformational change when it approaches each Trp residue at the same rate.

70 erized, including darobactin W3Y, with a non-Trp residue at the twice-modified central position, and

71 d by engineering a "Trp-zipper" protein with Trp residues at all 14 a and d positions.

72 gM) homodimer channels which have 4, 3, or 0 Trp residues at each end of the channel, respectively.

73 7-aza-Trp residues at either position showed a emission spectr

74 The Trp residues at either position showed nearly identical

75 We made five variants of RNase Sa by adding Trp residues at locations where they are found in other

76 ogs by fluorescence assays demonstrates that Trp residues at positions 401 and 402 are important for

77 Analogues of gramicidin A in which the Trp residues at positions 9, 11, 13, and 15 were sequent

78 In the present study we introduced trp residues at several other locations and examined the

79 By introducing additional Trp residues at strategic sites within a ligand-responsi

80 The common occurrence of Trp residues at the aqueous-lipid interface region of tr

81 uorescence analysis revealed that two native Trp residues at the membrane-proximal region of the coil

82 ress field distributions helps highlight the Trp residues at the protein/membrane/water interface as

83 Transmembrane helices with Trp residues at varying positions (and thus locating at

84 In the Mg2+-bound form of GCAP-1 all three Trp residues became more exposed to the polar environmen

85 f sensor via the simultaneous inclusion of a Trp residue but also as a turn-on sensor via the competi

86 ine dinucleotide (FAD) bound near a triad of Trp residues, but mutation of the terminal Trp in the tr

87 Specifically, we show that a proximal Trp residue can reduce bimane fluorescence intensity by

88 of the disordered tail lacking both Tyr and Trp residues causes a red shift in NEIL1's intrinsic Trp

89 icating that local structures around 6-(19)F-Trp residues change differently.

90 from substitution of a critical, interfacial Trp residue conserved at the intracellular base of TM1 (

91 Previous studies have shown that the Trp residue contributes to a high oxygen radical absorba

92 ays in E. coli show that introduction of the Trp residues does not block function of the channels.

93 R experiments, we show that only a subset of Trp residues engage in Ago interactions.

94 The three Trp residues equivalent to those in the N-lobe differed

95 uorescence studies indicated that all of the Trp residues exist in nonpolar environments that are hig

96 ncident with a light scattering decrease and Trp residue exposure, and independent of phosphorylation

97 Our findings suggest that the Trp residues flanking TM2, especially Trp-209, are impor

98 ll contained kynurenine residues in place of Trp residues found in the native apoprotein.

99 his method to identify and quantify reactive Trp residues from live cells.

100 The closest Trp residues (H52 and L35) are located approximately 17

101 TnC suggesting that the introduction of the Trp residue had no effect on the total secondary structu

102 appeared to lead to a conformation in which Trp residues had a higher degree of solvent exposure and

103 different positions have been replaced with Trp residues, has been investigated.

104 r molecules revealed in the proximity of the Trp residue have semiquantitative correlation with the o

105 icity, and the functional role(s) of its two Trp residues have been investigated.

106 of the mutant protein, we show that the two Trp residues have similar energy-transfer rates.

107 As inferred from the properties of the Trp residues, helices 1 and 5 appear to have the highest

108 uggesting retinoid interactions with Met and Trp residues, human recombinant CRALBP (rCRALBP) with al

109 e peptides bind phospholipids similarly, the Trp residue in 4F, 3F-1, and 3F-2 is less motionally res

110 d five single-Trp mutants, each containing a Trp residue in a different alpha-helix.

111 Taking advantage of a native Trp residue in ankyrin repeat (AR) 6 and engineered Trp

112 -coupled electron transfer akin to the axial Trp residue in cytochrome c peroxidase.

113 y brominated phospholipids suggests that the Trp residue in F80W-TbMscL is more exposed to the lipid

114 s more exposed to the lipid bilayer than the Trp residue in F93W-EcMscL.

115 The Trp residue in helix 2 is protected from the solvent but

116 allax analysis revealed that each engineered Trp residue in helix 4 of apoE3-NT, as well as those in

117 Thus, the conserved Trp residue in NOS may facilitate formation and/or react

118 ible to BrDM in the presence of TDG, while a Trp residue in place of Leu318 or Leu329 becomes more ac

119 l beta,d-maltoside (BrDM) demonstrate that a Trp residue in place of Val315, Val326, or Val331 become

120 esults of MD simulations, a highly conserved Trp residue in the A-helix of most repeat units that has

121 cal by intraprotein electron transfer from a Trp residue in the apoenzyme.

122 s in PMCA, whereas accessibility of the only Trp residue in the CaM-binding domain peptide was unalte

123 by the fluorescence emission lambdamax of a Trp residue in the center of the peptide sequence, the q

124 NQ2-5 channels, interacting with a conserved Trp residue in the channel pore domain.

125 By exciting a Trp residue in the coordination sequence, Tb(3+) bound t

126 The emission lambdamax of a Trp residue in the helix was used to determine its locat

127 he R-spine of RAF interacts with a conserved Trp residue in the vicinity of the NtA motif, connecting

128 The Trp residue in these motifs is located within 14 aa of t

129 with those from other species showed that a Trp residue in transmembrane domain V is the only transm

130 ence of the rate at which globally protected Trp residues in a protein react with HNSB is evaluated u

131 s definitive evidence for N-mannosylation of Trp residues in a protein.

132 hing studies with KI indicate that the three Trp residues in apoA-I-(44-186) are shielded from the aq

133 in fluorescence emission maximum of the two Trp residues in apoLp-III were observed in the pH range

134 idue in ankyrin repeat (AR) 6 and engineered Trp residues in AR2, AR4 and AR5, we show that the coope

135 rexpressed and was shown to prenylate C-3 of Trp residues in both linear and cyclic peptides in vitro

136 mide demonstrated an increase in exposure of Trp residues in both PITP(1-259) and PITP(1-253); bindin

137 In the belt model, the two Trp residues in each helix should exhibit maximal quench

138 ely 70% of total emission intensity of three Trp residues in GLTP and provides a stacking platform th

139 rescence quenching studies indicate that the Trp residues in helices 1 (N-terminal) and 5 (C-terminal

140 Larger quenching rates were observed for the Trp residues in helices 1, 4, and 5 than for those locat

141 Trp residues in helices 3 and 4 display the lowest mobil

142 Transthyretin has two Trp residues in its primary structure, Trp-41 and Trp-79

143 uorescence, indicating that the two pairs of Trp residues in LMM 77 are in different unfolding domain

144 ted peptide substrate (S4) and the intrinsic Trp residues in Lon to monitor peptide interacting with

145 determined that three of the seven available Trp residues in mature CPO are partially (40-50%) or com

146 rescence method for determining the depth of Trp residues in membrane-inserted polypeptides is introd

147 2)O(2) enhanced the solvent accessibility of Trp residues in PMCA, whereas accessibility of the only

148 peptides are generally better models for the Trp residues in proteins than NATA.

149 e current study, the role of the five C-lobe Trp residues in reporting the fluorescence change has be

150 ituted HDL (rHDL) to measure the position of Trp residues in single Trp mutants of human proapoA-I.

151 esonance energy transfer (FRET) from excited Trp residues in sLDLR to an extrinsic fluorophore covale

152 ency between either pCNPhe or pENPhe and the Trp residues in T4 lysozyme.

153 in neutralization potency, we conclude that Trp residues in the antibody H3 loop enable membrane pro

154 in which one or two of four highly conserved Trp residues in the binding tunnel had been replaced wit

155 The emission from Trp residues in the H subunit is partly quenched when de

156 Taking advantage of the Trp residues in the host protein, we first determined me

157 to the diverse local environments around the Trp residues in the individual proteins.

158 ly abolished 100% of the fluorescence of all Trp residues in the lipid-bound state.

159 rings the C-terminus of the protein near the Trp residues in the N-terminal half of the sequence.

160 ion on these intermediates, two of the three Trp residues in the protein were changed to Phe to gener

161 een ascribed to each of the three individual Trp residues in the protein.

162 The side chains of Trp residues in the three structures exhibit sequence-sp

163 g a more solvent-exposed environment for the Trp residues in the truncated protein, which also exhibi

164 might interact with the viral membrane, two Trp residues in this region were substituted separately

165 Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected pun

166 To address the role of the two Trp residues in Tva function, we prepared sTva harboring

167 intrinsic fluorescence of native tryptophan (Trp) residues in DnaB.

168 or the selective modification of tryptophan (Trp) residues in peptides and small proteins using elect

169 The tryptophan (Trp) residues in the original Trpzip1 sequence were syst

170 e quenching of the fluorescence of the three Trp residues indicated that Trp22 was the least exposed

171 hift and quenching experiments revealed that Trp residues inserted deeper into the hydrophobic enviro

172 Seven Trp residues inserted in varied microenvironments in the

173 y embedded Trp residues, suggesting that all Trp residues interact with the phospholipid acyl chains.

174 s cinereus peroxidase (CiP) by introducing a Trp residue into a heme peroxidase that has similar prot

175 spot residue Phe(279) Mutation of this HCDR3 Trp residue into any other residue except Tyr or Phe sig

176 the kinase through insertion of a conserved Trp residue into the active site.

177 We have introduced single Trp residues into the mechanosensitive channel of large

178 We have therefore introduced single Trp residues into the transmembrane regions of TbMscL an

179 Introduction of Trp residues into the Trp-devoid wild-type protein provi

180 1 through electrostatic interaction with the Trp residues involved in the functional activity of the

181 NMR spectra than LaP3W, indicating that the Trp residue is a critical hydrophobic anchor for maintai

182 are observed, which indicate that the single Trp residue is in a symmetric environment (most likely a

183 This crucial Trp residue is located deeper within transmembrane domai

184 obtained that the penultimate amino acid, a Trp residue, is especially important for subunit formati

185 in their structure three or four tryptophan (Trp) residues linked to a central scaffold.

186 s consistent with a belt model, because most Trp residues localized to a position about 5 A from the

187 ty, whereas those peptides with two or three Trp residues located adjacent to the cationic sector exh

188 osite the cationic sector, the peptides with Trp residues located adjacent to the cationic sector ind

189 The peptides with Trp residues located opposite the cationic sector displa

190 vealed that in contrast to the peptides with Trp residues located opposite the cationic sector, the p

191 of apomyoglobins with one or two tryptophan (Trp) residues located at invariant positions 7 and 14 in

192 Many membrane proteins contain more than one Trp residue, making analysis of the fluorescence data mo

193 ration for proteins that contain two or more Trp residues, mass spectroscopy analysis of peptides gen

194 eractions between the ribose protons and the Trp residues may contribute significantly to binding.

195 Within the Ago-binding domain, Trp residues mediate the direct interaction with the Ago

196 To better understand how Trp residues modulate the function of membrane-spanning

197 en of the n - 3 residues before the quenched Trps (residue n), are conserved in most crystallins.

198 and in the orientation of Trp91, a conserved Trp residue near the FMN chromophore.

199 eptides, having only one pair of interfacial Trp residues near either the amino or the carboxyl termi

200 cation-pi interaction between Lys(1) and the Trp residue nearest the C-terminus.

201 Three Trp residues occur naturally in the Escherichia coli Msc

202 mall molecule mimics of the monohydroxylated Trp residue of PreMADH also reacted with bis-Fe(IV) MauG

203 Replacement of either Trp residue of the ATP binding pocket with Phe or Leu de

204 sically presented MHC peptides, with the key Trp residue of the CDR3delta motif completing the defici

205 Unlike known UHMs that sequester the Trp residue of the ULM ligand in a hydrophobic pocket, S

206 By exciting Trp residues of CaD fragments or peptides while monitori

207 metal ions in the two domains of CaM and the Trp residues of CaD.

208 o investigate conformational exchange in the Trp residues of Hb A and the three mutant rHbs.

209 anges in local structure around four 6-(19)F-Trp residues of mADA were analyzed on the basis of the t

210 previously engineered by replacing the three Trp residues of native PNP with Tyr.

211 ons of membrane-embedded SybII, we show that Trp residues of the JMD influence the electrostatic surf

212 py and by the fluorescence properties of the Trp residues of this peptide.

213 Single-site Phe mutations of all nine Trp residues of thrombin enabled assignment of the fluor

214 magnetic resonance (ODMR) of the tryptophan (Trp) residues of alkaline phosphatase from Escherechia c

215 The indole ring of the critical penultimate Trp-residue of TRAP fits snugly into a newly formed hydr

216 lactamase L1 was engineered that contained a Trp residue on the loop to serve as a fluorescent probe.

217 transport since the distance between His and Trp residues on different helices is found to be short.

218 Here, we introduce Trp residues on either side of LacY where they are predi

219 Among Trp residues, only Trp-105, containing the most solvent-

220 proximately 1 kcal/mol, indicating that both Trp residues participate in interactions with ATP.

221 enzyme, the fluorescence of one of the three Trp residues per monomer is almost completely quenched,

222 Gramicidin A (gA), with four Trp residues per monomer, has an increased conductance c

223 tightly packed on the periplasmic side, and Trp residues placed at positions 245 (helix VII) or 378

224 Two Trp residues play pivotal roles for stabilizing MTHF by

225 Tryptophan (Trp) residues play important roles in many proteins.

226 esponding to each of the naturally occurring Trp residues (position -3 in the pro-segment, 8, 50, 72,

227 The fluorescence of a Trp residue positioned at the center of the hydrophobic

228 proline isomerization is involved, with the Trp residue presumably reporting on changes in its local

229 The location of these two Trp residues provides a unique method for analyzing stru

230 C-terminal to tyrosine (Tyr) and tryptophan (Trp) residues provides a potential alternative to enzyma

231 The location of Trp residues relative to the lipid bilayer was character

232 The location of the Trp residues relative to the lipid bilayer was investiga

233 th a Trp emission blue shift showed that the Trp residues remain largely shielded from the solvent wh

234 AF homology motif (UHM) and Bud13p harbors a Trp residue reminiscent of an UHM-ligand motif (ULM).

235 active site serine is mutated to an Ala and Trp residue, respectively.

236 We have identified a single tryptophan (Trp) residue responsible for loss of binding and biologi

237 ified mutant MscS proteins containing single Trp residues revealed that W16 and W251 are relatively i

238 These data suggest that the Na+,K+-ATPase Trp residue(s) involved in fluorescence energy transfer

239 Tyr and Trp residues served as donor and acceptor at the ends of

240 The picket fence model predicts that these Trp residues should be at different depths in the bilaye

241 e the same sequence as those surrounding the Trp residues studied in RNase Sa.

242 parable to that reported for deeply embedded Trp residues, suggesting that all Trp residues interact

243 ry1 physiological photocycle, we mutated the Trp residue that acts as the ultimate electron donor in

244 by monitoring the fluorescence signal from a Trp residue that is incorporated at a near-surface posit

245 nderstanding of the role of a conserved CarD Trp residue that serves as a minor groove wedge, prevent

246 hanges occur near a set of conserved His and Trp residues that are involved in proton gating.

247 vestigate the functional significance of the Trp residues that flank TM2 of Tar, we used site-directe

248 Binding entails insertion of Phe and Trp residues that project from one face of an alpha-heli

249 Converting each Trp residue to Phe and Gly by site-directed mutagenesis

250 to evaluate the contribution of each native Trp residue to the fluorescence changes observed during

251 e-directed mutagenesis of numerous conserved Trp residues to alanine had distinct effects.

252 ld help others in selecting sites for adding Trp residues to proteins.

253 We have added single Trp residues to RNase Sa at sites where Trp is found in

254 yl)sulfonium bromide (HNSB) with tryptophan (Trp) residues to measure protein folding free energies (

255 e protein Subtilisin Carlsberg, whose single Trp residue (Trp-113) was used as an intrinsic biologica

256 e interaction of QCN with TbHK1, as the lone Trp residue (Trp-177) was quenched under all conditions

257 crystal structural data shows a heavy chain Trp residue (Trp-H100) that is close ( approximately 3 A

258 iquinone through a set of 3 highly conserved Trp residues (Trp triad).

259 anslational modification of two constitutive Trp residues (Trp(beta)(57) and Trp(beta)(108) in Paraco

260 functional lactose permease mutant devoid of Trp residues (Trp-less permease).

261 ily conserved modifications to a sequence of Trp residues (Trp-triad) required for CRY photoreduction

262 One common feature is a key Trp residue, Trp(208) in LmP and Trp(191) in CCP, that i

263 hate remains more than 50 angstroms from any Trp residues until the final rate-determining conformati

264 anges in the spectroscopic properties of the Trp residues upon binding to lipid.

265 intensity and anisotropy of the COOH-domain Trp residues (W234, W236, and W285), which demonstrated

266 3 function by Ala replacement of a conserved Trp residue (W93A mutant) completely abolished STAT3 act

267 Using W39F as a template, a Trp residue was added to the flexile loop over the activ

268 A single Trp residue was introduced into the catalytic loop of Le

269 From this active construct, a single Trp residue was placed in the catalytic site loop (F159W

270 d new URP analogues in which the intracyclic Trp residue was replaced with natural, unnatural, and co

271 When either of the Trp residues was substituted with Tyr, the characteristi

272 tropy decay measurements suggested that both Trp residues were associated with substantial segmental

273 Single Trp residues were introduced into dIII by site-directed

274 The properties of the Trp residues were investigated by fluorescence spectrosc

275 The Trp residues were located in the nonpolar domains of the

276 nfirmed that most methionine (Met) and a few Trp residues were oxidized to various extents upon expos

277 directed mutants of the T domain with single Trp residues were prepared at the two naturally occurrin

278 fluorescence of Csk even though seven other Trp residues were present.

279 ered properties were created when any of the Trp residues were replaced by another amino acid, with t

280 tants in which three endogenous nonessential Trp residues were replaced by Phe residues, eliminating

281 The Trp residues were replaced with Tyr to produce Trp-free

282 pendently, mutants were constructed in which Trp residues were restricted to either the A or the B ch

283 the DAS of wild-type protein possessing two Trp residues were simulated well by that of one Trp muta

284 od agreement, although on average only three Trp residues were visited before emission.

285 n G, IgG) isotypes with oxidized tryptophan (Trp) residues were selectively generated by incubating t

286 F(1), or F(1) enzymes containing introduced Trp residues, were titrated with a soluble portion of th

287 indicate a different exposure of the EIAV MA Trp residues when bound to the two types of membranes, a

288 est this hypothesis, we modified Leu 98 to a Trp residue which is found in an endolysin from a bacter

289 in solvent accessibility of one of beta2m's Trp residues, which is buried during the initial structu

290 NOS contain a unique Trp residue whose side chain stacks with the heme and hy

291 of the binding to RNA due to stacking of its Trp residue with nucleic acid bases.

292 Replacing the neighboring Trp residue with phenylalanine removes these spectral pe

293 Cross-strand interacting Trp residues with an edge-to-face orientation had the st

294 the time-resolved fluorescence quenching of Trp residues with Cs+ ions.

295 their cognate target peptides containing 1-3 Trp residues with K(a) values in the range 1.7 x 10(4)-4

296 The relative positions of the Trp residues with respect to the phospholipid component

297 The interaction of the Trp residues with the lipid surface was investigated in

298 he active site of TrCel7A is lined with four Trp residues with two of them, Trp-40 and Trp-38, in the

299 markedly dependent upon the position of the Trp residues within the hydrophobic sector of an idealiz

300 modified by a dHexHex disaccharide, whereas Trp residues within three TSRs are also modified with C-