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 Each of its two ZFs has a Trp residue.

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

5 with the methyl group pointed toward another Trp residue.

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

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

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

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

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

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

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

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

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

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

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

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

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

19 little change in the microenvironment of the Trp residues.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

36 Trp residues and basic residues are abundant at the memb

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

55 The Trp residues are located in intrinsically disordered reg

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

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

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

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

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

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

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

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

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

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

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

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

68 7-aza-Trp residues at either position showed a emission spectr

69 The Trp residues at either position showed nearly identical

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

163 Seven Trp residues inserted in varied microenvironments in the

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

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

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

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

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

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

170 1 through electrostatic interaction with the Trp residues involved in the functional activity of the

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

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

173 This crucial Trp residue is located deeper within transmembrane domai

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

190 Three Trp residues occur naturally in the Escherichia coli Msc

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

213 Two Trp residues play pivotal roles for stabilizing MTHF by

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

252 3 function by Ala replacement of a conserved Trp residue (W93A mutant) completely abolished STAT3 act

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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