ライフサイエンスコーパス: hydrophobic amino acid

1 i (where X is any amino acid and varphi is a hydrophobic amino acid).

2 re hydrolysis occurs between proline and the hydrophobic amino acid.

3 -C-L/M-A-G-X-Psi-C, where Psi represents any hydrophobic amino acid.

4 tides starting with methionine followed by a hydrophobic amino acid.

5 germination machinery also recognizes other hydrophobic amino acids.

6 minus, showing a strong preference for large hydrophobic amino acids.

7 ) reading frames (RFs) that are enriched for hydrophobic amino acids.

8 ep pocket that includes both hydrophilic and hydrophobic amino acids.

9 ficantly more hydrophilic than Phe and other hydrophobic amino acids.

10 ural change upon binding Ca(2+) that exposes hydrophobic amino acids.

11 g the arginines, interacts with a cluster of hydrophobic amino acids.

12 interface is tightly packed and dominated by hydrophobic amino acids.

13 ein were replaced with random, predominantly hydrophobic amino acids.

14 -strands, wrapped around a core of conserved hydrophobic amino acids.

15 nd a loop that show an unusual clustering of hydrophobic amino acids.

16 segments with corresponding lengths of other hydrophobic amino acids.

17 with a high affinity for Lys, Arg and large hydrophobic amino acids.

18 t tyrosine-based motif followed by a pair of hydrophobic amino acids.

19 an der Waals' interaction with beta-branched hydrophobic amino acids.

20 abilization of the [4Fe-4S] cluster by bulky hydrophobic amino acids.

21 o acid preferring (BrAAP) cleave bonds after hydrophobic amino acids.

22 synthesis rather than cysteines, serines or hydrophobic amino acids.

23 emainder of the pore is wider and lined with hydrophobic amino acids.

24 elatin at the film surface and crosslink the hydrophobic amino acids.

25 port signal (NES), a leucine-rich stretch of hydrophobic amino acids.

26 nds directly C-terminal to basic, polar, and hydrophobic amino acids.

27 341 and Leu344 in the alpha-helix with other hydrophobic amino acids.

28 ducing a 5-fold decrease in k(cat)/Km toward hydrophobic amino acids.

29 r aromatic residues, but not by non-aromatic hydrophobic amino acids.

30 between the long-chain hydrocarbons and the hydrophobic amino acids.

31 aled that cocoa autolysates were abundant in hydrophobic amino acids.

32 The addition of a hydrophobic amino acid (A, L, or V) to the C terminus of

33 Subsequently, hydrophobic amino acids adjacent to each of the three fu

34 These key residues include Gln67, a small hydrophobic amino acid (Ala or Val) at the 57th position

35 charged aspartic and glutamic acids, and the hydrophobic amino acid alanine all destabilize mtDNA in

36 owed that substitutions with charged or less hydrophobic amino acids all reduced PLD activity.

37 phi)(T/S)(D/E)pY(G/A/S/Q) (where varphi is a hydrophobic amino acid and pY is phosphotyrosine).

38 T of Bacillus halodurans is a transporter of hydrophobic amino acids and a homologue of the eukaryoti

39 ir respective C2 domains bind via 2 pairs of hydrophobic amino acids and an amphipathic cluster.

40 model indicates a clear preference for bulky hydrophobic amino acids and for sulphur-containing amino

41 ionic carboxy-terminus residues that replace hydrophobic amino acids and have enhanced MHC binding, r

42 In addition, hydrophobic amino acids and negatively charged amino aci

43 Their sequences are rich in hydrophobic amino acids and strongly interact with lipid

44 c amino acids, with the highest affinity for hydrophobic amino acids and the lowest affinity for prol

45 yze N-acetyl and N-formyl derivatives of the hydrophobic amino acids and tripeptides.

46 motifs, YXXPhi (where Phi represents a bulky hydrophobic amino acid) and LL, that are important for b

47 es, which share an HbYX motif (where Hb is a hydrophobic amino acid) and open substrate access gates

48 ation of the gatekeeper residue (a conserved hydrophobic amino acid) and the use of a bulky inhibitor

49 contains evolutionarily conserved polar and hydrophobic amino acids, and mutations that change these

50 vinegar (BV) contains abundant essential and hydrophobic amino acids, and polyphenolic contents, espe

51 sport, 25 sites were individually mutated to hydrophobic amino acids, and the effect on proton transp

52 peat Sera Xxx Xxx Leud Xxx Xxx Xxx (Xxx is a hydrophobic amino acid) appears in both antiparallel hel

53 rboxyl terminus of UL20p, since aromatic and hydrophobic amino acids are known to be involved in prot

54 ltaDeltaG(0)w,i(pi)) residues and found that hydrophobic amino acids are most favorably transferred t

55 fluorescent protein (GFP) to the PM, and the hydrophobic amino acids are necessary for PM targeting o

56 ms that functionally important transmembrane hydrophobic amino acids are specified by codons containi

57 ated to the sequence HphiHphiHphiphi (phi, a hydrophobic amino acid), are a superfamily of nucleotide

58 rand distortion results in a solvent-exposed hydrophobic amino acid at residue 5.

59 To understand the influence of different hydrophobic amino acids at "a" and "d" positions of a he

60 ipeptide aldehydes were those that possessed hydrophobic amino acids at both the P1 and P2 positions.

61 Basic or hydrophobic amino acids at P1 and P1' positions in the s

62 preferentially phosphorylated peptides with hydrophobic amino acids at position +1 carboxyl-terminal

63 histidine at 201 while other species contain hydrophobic amino acids at position 201 in the otherwise

64 ell as the integrity of the highly conserved hydrophobic amino acids at positions 313-316, is essenti

65 with a pI of 5.5 that possesses 22 primarily hydrophobic amino acids at residues 3 to 25, predicting

66 Hydrophobic amino acids at S217, the last control cable

67 We identified a strong bias toward hydrophobic amino acids at T-cell receptor contact resid

68 thioether bond formation is specific toward hydrophobic amino acids at the acceptor site.

69 Our results demonstrate the importance of hydrophobic amino acids at the AT1R transmembrane interf

70 These enzymes were specific for hydrophobic amino acids at the C-terminus.

71 This suggests that hydrophobic amino acids at three conserved positions wit

72 and Val-scanning mutagenesis determined that hydrophobic amino acids at three homologous positions ar

73 in the presence of small amounts of racemic hydrophobic amino acid auxiliaries, which are known to b

74 utational analysis identified a stretch of 5 hydrophobic amino acids, AVAAV (amino acids 222-226), cr

75 ch is defined by a characteristic pattern of hydrophobic amino acids, basic and aromatic amino acids,

76 hypertriglyceridemia, two sets of conserved, hydrophobic amino acids between residues 261 and 283 wer

77 n analysis, and site-directed mutagenesis of hydrophobic amino acids between residues 290 and 311 all

78 vitro through a short sequence of basic and hydrophobic amino acids, BH site, based on the charge de

79 have polar amino acids on their surfaces and hydrophobic amino acids buried in their cores, protein e

80 s might therefore contain not only accepted "hydrophobic" amino acids, but also larger charged side c

81 P132G, P132W, P132F) revealed that no other hydrophobic amino acid can preserve the monomeric state

82 s of this study illustrate that conservative hydrophobic amino acid changes near the heme binding sit

83 pace to evaluate the effects of conservative hydrophobic amino acid changes on heme properties.

84 ,K-ATPase shows the presence of a relatively hydrophobic amino acid cluster proximal to N-glycosylati

85 by revealing the occurrence of drying inside hydrophobic amino acid clusters and its manifestation in

86 small number were not cysteine-rich but had hydrophobic amino acid clusters interspersed with argini

87 y the preferential incorporation of the more hydrophobic amino-acid component with increased rate and

88 conserved tip of Wnt's "index finger" forms hydrophobic amino acid contacts with a depression on the

89 g of the scaffolding region of caveolin to a hydrophobic amino acid-containing region within the regu

90 The cytoplasmic pore is lined by acidic and hydrophobic amino acids, creating a favorable environmen

91 Incorporation of hydrophobic amino acids D-Leu and D-Phe led to oligomeri

92 ement of the transmembrane domain with other hydrophobic amino acids did not impair growth.

93 eplacements of Ala and Gly with Arg or bulky hydrophobic amino acids displayed increased potency and

94 ed amino acid sequence, the protein contains hydrophobic amino acid domains at its N- and C-terminus

95 the salt bridge were replaced with strictly hydrophobic amino acids, E39M/K70M.

96 he substitutions of residue 481 with various hydrophobic amino acids elicited a profound alteration o

97 ated a limited number of substitutions, with hydrophobic amino acids especially interchangeable.

98 83-591), one side of which consists of three hydrophobic amino acids flanked by serine residues.

99 produced by substituting a varying number of hydrophobic amino acids for alanine on either one or bot

100 ns that substituted either smaller or larger hydrophobic amino acids for Val370, within the P2X2(a) s

101 A cluster of hydrophobic amino acids form a potentially cleavable sig

102 Hydrophobic amino acids forming alpha-helical structures

103 We further propose that the hydrophobic amino acids found between Lys100 and Pro141

104 ar residues except for a patch of relatively hydrophobic amino acids found in the carboxyl-terminal 1

105 rface recognition BHHB motif (B = basic, H = hydrophobic amino acid) found in protegrins and tachyple

106 k is composed of alternating hydrophilic and hydrophobic amino acids (glutamine and leucine, respecti

107 Two distinct activities cleaving bonds after hydrophobic amino acids have been identified in the bovi

108 room temperature, small organic solutes and hydrophobic amino acids have low solubilities in water a

109 isotropic model trend lines whereas those of hydrophobic amino acids (Ile, Phe) deviate positively fr

110 Two adjacent hydrophobic amino acids (Ile-2588 and Ile-2589) at the p

111 dependent receptor demonstrated that a large hydrophobic amino acid in this position promotes recogni

112 Mutational analyses of hydrophobic amino acids in ADM1 suggested that these res

113 3 amino acids, limits positively charged and hydrophobic amino acids in CDR3beta, and clonally delete

114 membrane (TM) domains to explore the role of hydrophobic amino acids in mediating specific interactio

115 In addition, hydrophobic amino acids in other positions were also cha

116 d in their structures sterically constrained hydrophobic amino acids in positions 6 (His) and 8 (Arg)

117 dreds of thousands of proteins consisting of hydrophobic amino acids in random order to isolate four

118 ctivities indicated that several charged and hydrophobic amino acids in ring B of bovicin HJ50, as we

119 In addition, substitution of bulky hydrophobic amino acids in series at the omega + 2 and o

120 g the overall ratio of positively charged to hydrophobic amino acids in surfactant protein B (SP-B),

121 interfacial region and prevents some of the hydrophobic amino acids in the alpha-helix from reaching

122 mutants and the solvent accessibility of the hydrophobic amino acids in the apo state, Ca(2+) bound s

123 localization was dependent on a sequence of hydrophobic amino acids in the extracellular domain of N

124 Alanine scanning revealed that hydrophobic amino acids in the first half of the tailpie

125 Strong preferences against certain hydrophobic amino acids in the hydrophobic positions wer

126 Replacement of the hydrophobic amino acids in the NES motif did not abolish

127 Here, we show that hydrophobic amino acids in the NS3 helix alpha(0) are re

128 Alanine substitution of individual hydrophobic amino acids in the NS3 helix alpha(0) impair

129 milarly, mutations disrupting four conserved hydrophobic amino acids in the p53 C-terminal NES block

130 trating individual substitutions of critical hydrophobic amino acids in the peptide resulted in the l

131 ndent binding sites containing two conserved hydrophobic amino acids in the S3b transmembrane segment

132 We have replaced all of the hydrophobic amino acids in the sequence of the helical d

133 The hydrophobic gasket (HG), a ring of hydrophobic amino acids in the voltage-sensing domain of

134 ared in a parallel series with all six bulky hydrophobic amino acids in their sequences replaced with

135 Similarly, hydrophilic substitution of two hydrophobic amino acids in this cluster disrupts both be

136 nstead hydrophobic in nature, five conserved hydrophobic amino acids in this region were also mutated

137 Thus, charged or hydrophobic amino acids in three regions of the MC159 DE

138 rved PhiXXPhiPhi motifs (with Phi denoting a hydrophobic amino acid) in AD1 and AD2.

139 tein surface and interact predominately with hydrophobic amino acids, in particular aromatic residues

140 at positions H24 in [I(6)F(13)H(24)](2) with hydrophobic amino acids incompetent for heme ligation.

141 Withdrawal of basic or hydrophobic amino acids induces translational repression

142 ds mostly interact with B-nucleotides, while hydrophobic amino acids interact extensively with A-nucl

143 rotein (Env) contains a stretch of conserved hydrophobic amino acids internal to its amino terminus (

144 ively fluorinated, or fluorous, analogues of hydrophobic amino acids into proteins potentially provid

145 Initially, we found that both basic and hydrophobic amino acids, irrespective of sequence, contr

146 eplacement of breakpoint serine with a bulky hydrophobic amino acid is sufficient to completely flip

147 The motif Pro-Asp-X-Asp, where X is a hydrophobic amino acid, is shown to be conserved among a

148 t, low-sensitivity receptor specific for the hydrophobic amino acids isoleucine, leucine, and valine.

149 led coil in N36(L6)C34 with a representative hydrophobic amino acid, isoleucine.

150 sidues were not critical or essential, three hydrophobic amino acids (L465, L476, and L480) played an

151 we identified a single stretch of conserved hydrophobic amino acids (LAM/LALRL/V (ScMcb1 228-234 and

152 A minimal tripeptide motif containing three hydrophobic amino acids (Leu, Val, and Ile) or any two p

153 A modified peptide 326 replacing hydrophobic amino acids leucine and tryptophan with neut

154 The aaRSs that activate the hydrophobic amino acids leucine, isoleucine, and valine

155 analyses suggest that the critical polar and hydrophobic amino acids localize on opposite sides of th

156 alysis also identified essential charged and hydrophobic amino acids located between two of the essen

157 diated by an annular determinant composed of hydrophobic amino acids located near the cytoplasmic end

158 The majority of these residues are hydrophobic amino acids located near the extracellular i

159 der Waals contacts with a group of conserved hydrophobic amino acids located on the rim of the C1 dom

160 drophobic contacts with a group of conserved hydrophobic amino acids located on the top half of the C

161 oplets are most likely domains of moderately hydrophobic amino acids located within the central 25% o

162 -based motif, YTKPhi (where Phi is any bulky hydrophobic amino acid), located between the second and

163 We tested this hypothesis by identifying two hydrophobic amino acids, M195 and F259, in the catalytic

164 pressure effects on the interaction between hydrophobic amino acids may be considerably amplified co

165 y active-site residues in enzymes, including hydrophobic amino acids, may contribute to catalysis thr

166 sylation by tryptophan 204 suggests that the hydrophobic amino acid mimics an ADP-ribosylated arginin

167 age is dependent upon the presence of paired hydrophobic amino acids; moreover, cleavage was found to

168 We also report a hydrophobic amino acid motif (GV) that, to date, is foun

169 first series, which retained the charge and hydrophobic amino acids of tachyplesin, but contained ze

170 is of integral membrane proteins (IMPs), the hydrophobic amino acids of the polypeptide sequence are

171 desolvation led to the exposure of embedded hydrophobic amino acids of WPI to riboflavin, facilitati

172 e hemifusion mutant that terminates with 15 (hydrophobic) amino acids of the HA TM domain, restored f

173 tinolytic activity, substrate preference for hydrophobic amino acids on both sides of the scissile bo

174 rk that linearizes the helix and exposes the hydrophobic amino acids on the opposite face of the heli

175 he isostere of lopinavir in combination with hydrophobic amino acids on the opposite P2/P2' position.

176 the exposed hydrocarbon chain interacts with hydrophobic amino acids on the surface.

177 odification of agPNA-peptide conjugates with hydrophobic amino acids or small molecule hydrophobic mo

178 ctures unless their sequences comprised more hydrophobic amino acids or until coordinating phosphate

179 of three subdomains, rich in either serine, hydrophobic amino acids, or glutamine.

180 The large hydrophobic amino acid p-benzoyl phenylalanine (pBzF) wa

181 There were 3-fold more hydrophobic amino acid pairs in HCV from nonresponding p

182 We prepared mutants in which the C2 domain hydrophobic amino acid pairs were changed to the homolog

183 r-X-Phi, where X is any residue and Phi is a hydrophobic amino acid) PDZ-binding interaction.

184 s of the genus Fusarium, is composed of four hydrophobic amino acids (Phe, two Leu, Val) and one hydr

185 The cluster of hydrophobic amino acids (Phe-5, Leu-6, and Val-9) on the

186 function because mutation of L343 to another hydrophobic amino acid, phenylalanine, in the beta2 AChR

187 Our results show that the N-terminal hydrophobic amino acids play an important role in the re

188 Biofilm formation was affected mostly by hydrophobic amino acid positions, suggesting that the ca

189 Here we show that the conserved hydrophobic amino acid preceding the phosphotyrosine is

190 membrane domain (TM) V and several primarily hydrophobic amino acids present within the cytoplasmic p

191 Mutagenesis of hydrophobic amino acids previously shown to contact the

192 R6Y containing additional cationic and bulky hydrophobic amino acids proved the best mimics of the am

193 Hydrophobic amino acid R groups are known to play a vita

194 d spikes 1 and 3, display four water-exposed hydrophobic amino acids, reminiscent of the membrane-int

195 mutant receptors, particularly those with a hydrophobic amino acid replacement, may not bind CheW/Ch

196 esidues 1-72) that includes a sequence of 20 hydrophobic amino acids required for membrane translocat

197 nstitutive activity, suggesting that a large hydrophobic amino acid residue at position 254 alters tr

198 conserved CxxxC motif (where "x" can be any hydrophobic amino acid residue) in physical interactions

199 Several hydrophobic amino acid residues are important recognitio

200 Site-directed mutagenesis revealed that hydrophobic amino acid residues centrally located in the

201 lycosylhydrolases, including both acidic and hydrophobic amino acid residues critical for enzyme acti

202 promoters; (ii) assess the role of conserved hydrophobic amino acid residues for MarA activity; and (

203 One mutant, with replacements at three hydrophobic amino acid residues in the C-terminal domain

204 110 (amino acid 1-308) and CREB to conserved hydrophobic amino acid residues in the CAD.

205 Repositioning of mostly hydrophobic amino acid residues in the core of the C-ter

206 interactions of Arg120, Tyr355, and several hydrophobic amino acid residues in the COX-2 active site

207 s in mussel plaques), the high proportion of hydrophobic amino acid residues in the flanking sequence

208 Mutations of positively charged and hydrophobic amino acid residues in the IIS4 segment do n

209 roduction of highly fluorinated analogues of hydrophobic amino acid residues into proteins has proved

210 ional analyses revealed that three blocks of hydrophobic amino acid residues located within TAND3 are

211 Ga-Pa-PCNA1 complex is thermostable, and two hydrophobic amino acid residues on Pa-UDGa (Phe(191) and

212 We have identified five hydrophobic amino acid residues on the ALK4 extracellula

213 They further predict that specific hydrophobic amino acid residues on the nonglycosylated G

214 tween helices of a coiled coil are formed by hydrophobic amino acid residues packed in a "knobs-into-

215 XTEN lacks hydrophobic amino acid residues that often contribute to

216 te-directed mutagenesis to change charged or hydrophobic amino acid residues to alanines to identify

217 that this leucine may interact with several hydrophobic amino acid residues to influence the spatial

218 or silk proteins is a strong predominance of hydrophobic amino acid residues to provide for the hydro

219 This specificity for hydrophobic amino acid residues was corroborated by inhi

220 viously suggested role of a stretch of small hydrophobic amino acid residues within the first transme

221 on defects resulted solely from mutations of hydrophobic amino acid residues within the hydrophobic c

222 d a conserved C-terminal primary anchor with hydrophobic amino acid residues, as well as one or more

223 ccurs primarily through aromatic, basic, and hydrophobic amino acid residues, the majority of which a

224 peptide, contains a high ratio of charged to hydrophobic amino acid residues.

225 acid residues 154-193), which contains many hydrophobic amino acid residues.

226 f its heptad a positions are not occupied by hydrophobic amino acid residues.

227 ce showed a clear demarcation of charged and hydrophobic amino acid residues.

228 ts the solvent-mediated interactions between hydrophobic amino-acid residues.

229 Mutation of the hydrophobic amino acids resulted in nuclear accumulation

230 Replacement of this Asn202 with a variety of hydrophobic amino acids results in a protein that is bli

231 een the nucleus and cytoplasm, using typical hydrophobic amino acid-rich nuclear export sequences, an

232 ween authentic signal sequences and the less hydrophobic amino acid segments in cytosolic proteins.

233 However, the relationship between the hydrophobic amino acid sequences of transmembrane domain

234 e targeting and membrane insertion of highly hydrophobic amino acid sequences.

235 Shape-complementary clustering of hydrophobic amino acids, several of which participate in

236 The length of the hydrophobic amino acid side chain at position 144 appear

237 rms specific favorable interactions with the hydrophobic amino acid side chain, alpha-carbon, carboxy

238 ns is caused by disruption of the cluster of hydrophobic amino acid side chains and that the midregio

239 Several hydrophobic amino acid side chains are positioned near t

240 ix may function to force solvent exposure of hydrophobic amino acid side chains in the regions flanki

241 d gate in the ion-conducting pore, formed by hydrophobic amino acid side chains, located ~60 angstrom

242 of N-Hsp90 with the concomitant exposure of hydrophobic amino acid side chains.

243 s, whereas denaturation was much slower with hydrophobic amino acid side chains.

244 adheres to the outer forespore membrane via hydrophobic, amino acid side-chains on the hydrophobic f

245 e, X is any amino acid, and phi is any bulky hydrophobic amino acid) signal sequence (YSRV) that medi

246 es for PKA and PKC and are rich in basic and hydrophobic amino acids similar to a class of membrane-t

247 t that CaM recognizes a '1-4-7-8' pattern of hydrophobic amino acids starting at Trp79 in AKAP79.

248 known low density lipoprotein receptor, a 24 hydrophobic amino acid stretch spanning the plasma membr

249 As a hydrophobic amino acid-substituted ATPase, YchF does not

250 e of a catalytic His is also observed in the hydrophobic amino acid-substituted GTPase RbgA and is an

251 show that several phospholamban mutants with hydrophobic amino acid substitutions at the Leu/Ile zipp

252 Mutants with more hydrophobic amino acid substitutions fold faster, and th

253 bstitutions fold faster, and those with less hydrophobic amino acid substitutions fold slower.

254 All hydrophobic amino acid substitutions were transforming w

255 head composed of aspartic acid and a tail of hydrophobic amino acids such as alanine, valine, or leuc

256 teins incorporating fluorinated analogues of hydrophobic amino acids such as leucine and valine into

257 The alternating pattern of hydrophilic and hydrophobic amino acids suggests the possibility that SB

258 We find that three of the five hydrophobic amino acids targeted in these loops, tryptop

259 The contents of free hydrophobic amino acids, taurine and carnosine/anserine

260 Here we identify a hydrophobic amino acid tetrad (ILLV) close to the C term

261 Substitution of the conserved hydrophobic amino acid that was located two residues N-t

262 is achieved via a noticeable arrangement of hydrophobic amino acids that are exposed at the surface

263 Hydrophobic amino acids that contribute to trimer format

264 c sequences of leucines and isoleucines, two hydrophobic amino acids that differ only by the position

265 e identify highly conserved carboxy-terminal hydrophobic amino acids that function as a leptomycin B-

266 The N-terminal domain rich in hydrophobic amino acids that is predicted to form a hydr

267 istal cavity of DHP is surrounded by several hydrophobic amino acids that stabilize internal binding

268 m di-hydrophobic (TDH) motif, where Phi is a hydrophobic amino acid), the signal shows no resemblance

269 Together with other hydrophobic amino acids, the phenylalanines act as the c

270 en the (329)RKK(331) residues are mutated to hydrophobic amino acids, these residues form even strong

271 in PHAS-I and the h(S/T)h site (where h is a hydrophobic amino acid) Thr389 in p70(S6K), were phospho

272 c residues), the viral cytokine largely uses hydrophobic amino acids to contact gp130, which enhances

273 sine, ornithine, histidine and arginine, the hydrophobic amino acid tryptophan, and alanine as a spac

274 including branched-chain amino acids, other hydrophobic amino acids, tryptophan breakdown products,

275 The contribution of a hydrophobic amino acid two residues upstream of the tyro

276 Two hydrophobic amino acids, Tyr4 and Trp13, appear essentia

277 axseed protein structure since exposition of hydrophobic amino acid tyrosine was modified.

278 Mutation of lysine residues to hydrophobic amino acids, tyrosine or alanine, leads to i

279 itutions of leucine at position 492 with the hydrophobic amino acids valine or phenylalanine also red

280 Mutation of most of the nonpolar or hydrophobic amino acids (W174, F175, G176, Y179, and A26

281 ensus motif GHFGGXY, where X is preferably a hydrophobic amino acid, was shown previously to inhibit

282 Three large hydrophobic amino acids were conserved; analogues of the

283 Aromatic and bulky hydrophobic amino acids were effective substitutes for e

284 Hydrophobic amino acids were tolerated in functional rec

285 ible hydrophilic residues were replaced with hydrophobic amino acids, were shown to still assemble pr

286 -Tyr-Tyr-X-Tyr cluster, where X represents a hydrophobic amino acid, which terminates with acidic res

287 ading frame use resulting in predominance of hydrophobic amino acids, which are counterselected in co

288 15-LOX-2 contains a long loop, composed of hydrophobic amino acids, which projects from the amino-t

289 G(unfold)) afforded by the substitution of a hydrophobic amino acid with its fluorinated analogue var

290 gh concentration solutions of a prototypical hydrophobic amino acid with its polar backbone, N-acetyl

291 at position 8 and replacement of C-terminal hydrophobic amino acids with basic residues.

292 Replacing hydrophobic amino acids with charged residues in beta-st

293 hypothesis, we exchanged the remaining three hydrophobic amino acids with neutral amino acids by site

294 tein, ranging from long-chain fatty acids to hydrophobic amino acids, with EC(50) values from 99 nM f

295 Conserved hydrophobic amino acids within the cysteine-rich region

296 Hydrophobic amino acids within these motifs have been id

297 Both acidic and hydrophobic amino acids within this activation domain we

298 GRK5 and define the importance of a group of hydrophobic amino acids within this motif in mediating i

299 of the p10 sequence and identified the four hydrophobic amino acids within this region that comprise

300 PI31 has a C-terminal HbYX (where Hb is a hydrophobic amino acid, Y is tyrosine, and X is any amin