ライフサイエンスコーパス: helical conformation

1 zing that portion of the S4 segment in alpha-helical conformation).

2 which we reveal adopts a predominantly alpha-helical conformation.

3 ER based on their ability to adopt an alpha-helical conformation.

4 rged lipid membranes while adopting an alpha-helical conformation.

5 ly forms an imperfect polyproline (polyP) II helical conformation.

6 t beta conformations and stabilize the alpha-helical conformation.

7 s not strictly favor the previously proposed helical conformation.

8 ures, notably the all-cis polyproline I-like helical conformation.

9 ucture with a previously unidentified triple helical conformation.

10 entially locking caspase-6 into the inactive helical conformation.

11 uce the foldamer to collapse into a presumed helical conformation.

12 o forego a coil state and join a preexisting helical conformation.

13 mulations that reveal and confirm the double helical conformation.

14 ype of helix formed and the stability of the helical conformation.

15 to lock this unstable region into the triple helical conformation.

16 a s protein) of the peptide adopted an alpha-helical conformation.

17 t completely disordered, but adopt a partial helical conformation.

18 adopt the left-handed polyproline II (P(II)) helical conformation.

19 helix from C9 and an overall decrease of the helical conformation.

20 mutations suggested that IL2 is in an alpha-helical conformation.

21 cceptors at neutral pH and disrupt the alpha-helical conformation.

22 ophases in which the peptides adopt an alpha-helical conformation.

23 e segment 5 (TM5i) in either an unwound or a helical conformation.

24 parameters that offer precise depiction of a helical conformation.

25 ation may not significantly stabilize the 12-helical conformation.

26 raining short peptides typically in an alpha-helical conformation.

27 n bind membranes in either a disordered or a helical conformation.

28 ne attachment augments the distortion in DNA helical conformation.

29 mbrane-bound alpha-synuclein adopts an alpha-helical conformation.

30 receptors, with the peptides in amphipathic helical conformations.

31 hey do not exhibit a substantial sampling of helical conformations.

32 HCl, the combined data are well fit by alpha-helical conformations.

33 ptides showed only the i,i+3 hydrogen-bonded helical conformations.

34 NMR studies reveal that human amylin samples helical conformations.

35 rts between energetically degenerate P and M helical conformations.

36 handed (alpha(R)) and left-handed (alpha(L)) helical conformations.

37 r admixtures of beta-strand and right-handed helical conformations.

38 quences that do not spontaneously form alpha-helical conformations.

39 dominated by pathways that visit metastable helical conformations.

40 can induce peptides and proteins to take up helical conformations.

41 aining M2 and correspond to more ideal alpha-helical conformations.

42 lded, with exchange between beta strands and helical conformations.

43 bilizing a region of the S4 segment in alpha-helical conformation, a closed (resting or intermediate)

44 ical conformation distinct from the extended helical conformation adopted when alphaS is bound to int

45 ylation to determine if stabilization of CUG helical conformations affected toxicity.

46 The helical conformation aligns residues to form an amphipat

47 ound complex, eight residues of Gcn4 adopt a helical conformation, allowing three Gcn4 aromatic/aliph

48 ations on the Abeta(42) monomer at its alpha-helical conformation and a pentamer fibril fragment of A

49 es: a closed DNA gate in a B-A-B form double-helical conformation and a second B-form duplex associat

50 t structural environments: a disordered 3(1)-helical conformation and an ordered beta-sheet structure

51 esidues 117-137) adopts a well defined alpha-helical conformation and binds 14-3-3 in a phosphorylati

52 erestingly, HCDR1 of MAb 3.1 adopts an alpha-helical conformation and engages in hydrophobic interact

53 d GalR2, respectively), logD = 1.24, minimal helical conformation and improved metabolic stability.

54 hat the rationally designed peptide adopts a helical conformation and is capable of disrupting KSHV P

55 gh-resolution structures of the basic triple-helical conformation and its water-mediated hydration ne

56 conformational fluctuations between a folded helical conformation and one or more locally unfolded st

57 e 3FD-IL displays 3-fold screw symmetry in a helical conformation and self-assembles into nanosheets

58 al molecules of monomeric alphaS in an alpha-helical conformation and that such channels may have a r

59 nsensus sequence is consistent with an alpha-helical conformation and that these residues maintain ex

60 f both lysine 4 and lysine 9 reduce both the helical conformation and the stability of the most popul

61 ased circular dichroism to confirm its alpha-helical conformation and transmembrane alignment.

62 ion patterns reported for other nucleic acid helical conformations and provides support for the great

63 ces, because beta-peptides adopt predictable helical conformations and resist proteolysis.

64 that W41F M2 retains the pH-dependent alpha-helical conformations and tetrameric structure of the wi

65 n this work are shown to exhibit stable H-14 helical conformations and, in some cases, relatively sta

66 enhancement buildup points to a large alpha-helical conformation, and a distinct increase in fluores

67 Residues 446-456 exhibited a propensity for helical conformation, and an extended conformation follo

68 in peripherin-2 binds to membranes, adopts a helical conformation, and promotes membrane fusion, whic

69 such an interruption for the collagen triple-helical conformation, and provides insight into possible

70 A-SP1 junction region spontaneously adopts a helical conformation, and the proteins associate into te

71 on is the most stable, followed by the alpha-helical conformation, and then the unstructured coil.

72 revealed features characteristic of an alpha-helical conformation approximately approximately 15-19 r

73 Water-soluble peptides that adopt stable helical conformations are attractive motifs because of t

74 Previously we concluded that two helical conformations are available to 2:1 and 1:2 alpha

75 onal structural and dynamical aspects of the helical conformations are explored, with a focus on cont

76 We conclude that this sampling of helical conformations arises from the context dependence

77 Mouse aS exhibits a higher propensity to helical conformation around the C-terminal substitutions

78 The peptide agonist retains an alpha-helical conformation as it sits deep within the receptor

79 1 is highly flexible and capable of assuming helical conformations (as in the postfusion helical bund

80 entration Con A transforms to a highly alpha-helical conformation at both neutral and low pH.

81 d state at low [TFE] and with a highly alpha-helical conformation at high [TFE].

82 and the 3'-OH base pair and distorts the DNA helical conformation at the nick.

83 ordered melittin monomers at low pH to alpha-helical conformations at neutral pH occurs on nearly the

84 xtended conformations are favored over alpha-helical conformations at the dipeptide level at and belo

85 allow a detailed characterization of the 12-helical conformation; average backbone torsion angles of

86 tion of a H(+)-stabilized intermediate alpha-helical conformation before aggregation develops.

87 nally flexible region of gp41 assumes mostly helical conformations but adopts a kinked, extended stru

88 revealed that this region can adopt an alpha-helical conformation, but that this folding requires neu

89 ta(42) peptide (residues 17-21) to its alpha-helical conformation by interacting specifically in this

90 s predominantly disordered but samples alpha-helical conformations covering residues 15-24 and 29-35

91 ted segment in the S1 domain adopts an alpha-helical conformation, despite being predicted to be nati

92 ons is their ability to drive transitions to helical conformations different from canonical B-form DN

93 hat in nanoparticles alphaS assumes a broken helical conformation distinct from the extended helical

94 60-71), DKNPFKELKGGC, assumes an amphipathic helical conformation during interaction with metarhodops

95 ructure is that the autolysis loop assumes a helical conformation enabling W148 and W215, located 17

96 Conantokin-Pr3 adopts an alpha-helical conformation even in the absence of divalent cat

97 These polymers, known to adopt helical conformations, exhibited ordered surface coverag

98 ree MPER peptides each adopt symmetric alpha-helical conformations exposing the amino acid side chain

99 nsistently show folding of the A-loop into a helical conformation followed by unfolding to an active

100 en the N and the C termini of the CRD, and a helical conformation for the last repeat.

101 Besides providing evidence of a folded helical conformation for the peptide bridge, IR and NMR

102 of accessibility is consistent with a alpha-helical conformation for this segment of TMH6.

103 used to study the thermodynamic stability of helical conformations formed by beta-peptides containing

104 l-suited and straightforward for PASs as the helical conformations formed result from constraints imp

105 he helical state and that the number of pure helical conformations found at room temperature is great

106 The unphosphorylated peptide maintains a helical conformation from 3 to 15 throughout a 26-ns sim

107 A-L-A segment in the context of a continuous helical conformation from an aqueous environment into th

108 upon membrane-association result in a alpha-helical conformation from K6 to F17, i.e., up to the ver

109 ix 12, which can result in an extended alpha-helical conformation, further accelerates lipid-mixing.

110 helices, with the macrocycle templating the helical conformation having a significant influence.

111 ha-helical region and induces a unique alpha-helical conformation in Abeta.

112 tion in neutral and basic media and an alpha-helical conformation in acidic media, the helical conten

113 es predisposing the peptide toward the alpha helical conformation in an effort to enhance the reactiv

114 ysis shows the alt-PASs adopt a right-handed helical conformation in aqueous solutions.

115 also embedded but deviate from linear alpha-helical conformation in contrast to I693-K716, which clo

116 teraction and the novel membrane-bound alpha-helical conformation in IAPP aggregation are discussed.

117 peptide chains, adopts a predominantly alpha-helical conformation in its native state.

118 BM2 adopts an alpha-helical conformation in lipid membranes.

119 -7 to Phe-11 region of HFPtr has predominant helical conformation in membranes without cholesterol an

120 nt stapled peptide, DD5-o, revealed an alpha-helical conformation in methanol, stabilized by an unusu

121 Our results show that FK1TMD adopts a stable helical conformation in phosphatidylcholine lipids when

122 amma-peptide foldamers that adopt a specific helical conformation in solution and in the solid state.

123 d that the purified TP adopted more than 50% helical conformation in solution but also showed that th

124 have a strong tendency for adopting an alpha-helical conformation in solution.

125 tive-site alpha6' helix, which would adopt a helical conformation in the active R-state and a less st

126 sm (CD) spectra, while the handedness of the helical conformation in the BCP* is determined from a sp

127 e, prove that the peptide is in an all alpha-helical conformation in the bilayers of multilamellar ve

128 of CD152 adopts a polyproline type II (PPII) helical conformation in the CD80-CD152 complex.

129 transitions of extracellular loop 2 from the helical conformation in the D(2)R/risperidone structure

130 Here we report a double helical conformation in the densely charged aromatic pol

131 subcomplex shows that ARP binding induces a helical conformation in the helicase-SANT-associated (HS

132 ar and frayed first helix (Helix C'); (ii) a helical conformation in the junction region connecting H

133 ransmembrane domain of CYPOR adopts an alpha-helical conformation in the lipid membrane environment.

134 he MSD peptide assumes a stable tilted alpha-helical conformation in the membrane.

135 The S4 segment has a 3(10)-helical conformation in the narrow inner gating pore, wh

136 The PET domain adopts a helical conformation in the presence of 2,2,2-trifluoroe

137 e, it undergoes a structural transition to a helical conformation in the presence of a variety of mul

138 TIRAP PBM transitions from a disordered to a helical conformation in the presence of either zwitterio

139 ed in solution and only folded into an alpha-helical conformation in the presence of liposomes.

140 ular dichroism spectroscopy showed a similar helical conformation in the presence of the anionic lipo

141 Overall, the data favour a helical conformation in the super-repeat.

142 odicity of approximately 3.5-4, indicating a helical conformation in the two scanned regions (residue

143 The bound peptide adopts a helical conformation in which the key contact residues,

144 s suggest that the G13L mutant adopts a less helical conformation in which the N-terminus moves close

145 nformational equilibrium was shifted towards helical conformations in Ac-Aib-Ala-Ala-OMe, indicating

146 TPA(+) stabilizes helical conformations in alahel peptides, indicating exc

147 10 residues, different from the well-defined helical conformations in all other known structures, ind

148 esting the b10 is the lower limit for stable helical conformations in b ions.

149 etween these forms allows adopting different helical conformations in different nucleotide states.

150 surements demonstrated the retention of main helical conformations in immunogenic formulations based

151 ; both peptides adopt nearly identical alpha-helical conformations in the complexes, where the three

152 Conantokins-Pr1 and -Pr2 adopt alpha-helical conformations in the presence of divalent cation

153 ese five beta-peptides adopt fully folded 12-helical conformations in the solid state.

154 -bRs have quantifiable preferences for alpha-helical conformations in their unbound monomeric forms.

155 Many host-defense peptides adopt alpha-helical conformations in which cationic side chains and

156 re achiral peptides that typically adopt 310 helical conformations in which enantiomeric left- and ri

157 ligomers of the achiral amino acid Aib adopt helical conformations in which the screw-sense may be co

158 own that o-phenylenes fold into well-defined helical conformations (in solution and, typically, in th

159 Double-stranded DNA and RNA adopt different helical conformations, including the unusual Z-conformat

160 when kafirin was dissolved in GAA its alpha-helical conformation increased substantially.

161 association, whereas stabilization of alpha-helical conformation inhibits beta-sheet formation.

162 r binding affinity and thus stabilizes alpha-helical conformations intermediately between NaClO(4) an

163 The right-handed helical conformation is engineered into the polymers by

164 The relative abundance of the helical conformation is found to vary as a function of p

165 the ability to adopt a globally amphiphilic helical conformation is not a prerequisite for selective

166 suggests that an internally hydrogen-bonded helical conformation is partially populated in solution.

167 Furthermore, its helical conformation is required for this function.

168 Con-T can be attributed to the fact that its helical conformation is stabilized by charge-charge inte

169 A preference for helical conformations is observed at close encounter bet

170 igands around the Cr(III) provided nonplanar helical conformations leading to the diastereoselective

171 l cyclic CRF bind to the ECD1 of CRF-R1 in a helical conformation mainly along the hydrophobic face o

172 nterferes with export, which suggests that a helical conformation may be important.

173 Further, the acquired helical conformation may explain why the peptide seems t

174 e kafirin molecules in GAA, assuming a alpha-helical conformation may have enhanced water binding, en

175 conditions that promote weakly stable alpha-helical conformations may promote IAPP aggregation.

176 the N-terminal region lid region bound in a helical conformation mimicking the bound structure of p5

177 dienone are required in order to produce the helical conformation needed to generate a single diaster

178 analyses suggested that the MLV CAH forms a helical conformation, no structural or biochemical data

179 to Phe(CN) mutation alters neither the alpha-helical conformation nor the 4-helix bundle structure.

180 6-227), retaining the disulfide-linked alpha-helical conformation observed in the normal cellular iso

181 ene building block, resulted in the specific helical conformation of 22-hetero-1,5-naphthiporphyrins.

182 The presence of a two- and four-turn helical conformation of 8 and 9, respectively, in polar

183 oxyglutamic acid residues in stabilizing the helical conformation of conantokins, we designed, synthe

184 lar dichroism experiments confirmed that the helical conformation of conRl-B is stabilized by divalen

185 without disturbing the poly-proline type II helical conformation of each chain.

186 or the first time that MOZ DPF induces alpha-helical conformation of H3K4-T11, revealing a unique mod

187 esented that stabilizes a pre-amyloid, alpha-helical conformation of IAPP.

188 An alpha-helical conformation of PAP(248-286), lying parallel to

189 nstead, it recognizes the intrinsic stacked, helical conformation of poly(A) RNA.

190 and characterizes, therefore, the dominating helical conformation of tercyclopropanedimethanol with a

191 cated that Ab6E2 specifically recognizes the helical conformation of the acidic stretch.

192 ed structure as opposed to the predominantly helical conformation of the full-length antifungal pepti

193 an agonist and the ECD1-CRF-R1 promotes the helical conformation of the N terminus of the former, im

194 t phosphorylation at T3 stabilizes the alpha-helical conformation of the N-terminal 17 amino acids (N

195 The predominantly alpha-helical conformation of the peptide alone at pH5-6.5 was

196 lating divalent cations induce and stabilize helical conformation of the peptide.

197 mellar vesicles were used to corroborate the helical conformation of the peptides found in detergent

198 aminoproline derivatives on the local triple helical conformation of the peptides.

199 NMR-based analysis reveals a helical conformation of this fragment that utilizes its

200 ineered metal ion site, stabilizing an alpha-helical conformation of this loop segment.

201 The helical conformation of this motif provides a structural

202 e is believed to stabilize an extended alpha-helical conformation of this peptide while in solution a

203 For helical conformations of lengths shorter than eight resi

204 -Ala-Ala-OMe, indicating that Aib can induce helical conformations of neighboring residues positioned

205 understand common observations, such as the helical conformations of the pellicle, and identify prev

206 region, which is predicted to adopt an alpha-helical conformation on membrane contact.

207 hage proteins to nucleate pVIII in the alpha-helical conformation on the DNA.

208 assumed model where alphaS lies in an alpha-helical conformation on the membrane surface and instead

209 gion systematically prefers a straight alpha-helical conformation once embedded in a membrane bilayer

210 Of the micellar ensemble of helical conformations only a limited set agrees in quant

211 The 3(10) helical conformation orients the gating arginines on S4

212 icon resulting in a higher population of one helical conformation over another.

213 ferent G-patch proteins, transiently samples helical conformations, possibly facilitating a conformat

214 as a dimer to the dodecapeptide in an alpha-helical conformation, predicated on a substantial struct

215 finite and perhaps limited repertoire of RNA helical conformation preferences.

216 ructurally polymorphic as it can also form a helical conformation recognized by RV144 vaccine-induced

217 ing that it may form the polyproline type II helical conformation required for SH3 docking only in th

218 ts 3 and 4, stabilizing the loop in an alpha-helical conformation required to engage the G protein.

219 apability (up to 5-fold) by fixing the alpha-helical conformations required for optimal receptor inte

220 e highly stable carbocations with planar and helical conformations respectively.

221 carbons populate regular and less-controlled helical conformations, respectively.

222 and i, i + 7 pairs, to favor 3(10)- or alpha-helical conformations, respectively.

223 The dipole moments associated with alpha-helical conformations show the best alignment with the e

224 inked di-, tri-, and tetramannosides bind in helical conformations similar to the solution global min

225 lpha-derived sequence was induced into alpha-helical conformation, suggesting that conformation plays

226 x II exhibits little evidence for adopting a helical conformation, suggesting that this region is a l

227 ergent complexes show a repertoire of curved helical conformations, suggesting multiple helical arran

228 e interaction sites exhibit a preference for helical conformations, suggesting that these sites adopt

229 had similar FTIR spectra, with greater alpha-helical conformation, than the kafirin preparations whic

230 ial surface, where this peptide adopts alpha-helical conformations, than cholesterol-enriched LUVs mi

231 The alpha/beta-peptide foldamer adopts a helical conformation that displays a catalytic primary a

232 This motif adopts a stable helical conformation that docks onto a GAL1 hydrophobic

233 he peptides assume a membrane-spanning alpha-helical conformation that does not disrupt bilayer integ

234 ate that these tripyrrolic systems take on a helical conformation that favors macrocycle formation, a

235 This caspase-6 region can also adopt a helical conformation that has not been seen in any other

236 The arrested NC adopts a compact alpha-helical conformation that induces 28 S rRNA nucleotide r

237 the C-terminal residues are confined to the helical conformation that is found in the x-ray structur

238 azobenzene leads to a distortion of the DNA helical conformation that is similar for the trans and c

239 licate balance to maintain pVIII in an alpha-helical conformation that requires either an oriented bi

240 kely than the false positives to adopt alpha-helical conformations that transition to loops at their

241 IP adopts a well-defined transmembrane alpha-helical conformation the peptide still exhibits heteroge

242 In the helical conformation, the two basic residues are well se

243 he meso oligomers adopt chiral canonical 2.5-helical conformations, the equally populated enantiomeri

244 e binding of a C-terminal extension in alpha-helical conformation to a pocket next to the active site

245 , our data indicates that S4 undergoes alpha-helical conformation to a short-lived different secondar

246 t direct evidence of a conversion from alpha-helical conformation to beta-sheet fibrils in the presen

247 DAXX uses an extended alpha-helical conformation to compete with major inter-histone

248 alkane accommodated, n-tetradecane, adopts a helical conformation to fit in the cavity, a shape that

249 meric or small oligomeric forms of SEVI in a helical conformation to lipid membranes may be an additi

250 (PrPSc), shifting from a predominantly alpha-helical conformation to one dominated by beta-sheet stru

251 -solid preparations, where gelatin maintains helical conformation to provide network integrity as wel

252 lature) of Cgb adopts a highly ordered alpha-helical conformation unlike any previously characterized

253 We show that the gating brake assumes a helical conformation upon binding CaM, with associated c

254 11-31 complex reveals that TCTP refolds in a helical conformation upon binding the BH3-groove of Bcl-

255 flexible catalysts adopt a reinforced chiral helical conformation upon binding to a chloride anion, a

256 It folds into an alpha-helical conformation upon binding to anionic (but not zw

257 conformation in solution and adopts an alpha-helical conformation upon binding to lipid membranes.

258 c-region of the signal peptide form an alpha-helical conformation upon binding to SecA.

259 es, most of which adopt an amphipathic alpha-helical conformation upon binding to the lipids.

260 undergoes a transition from a random coil to helical conformation upon encountering synaptic vesicle

261 ntegrity to ultimately adopt the preferred P-helical conformation upon hybridization with DNA.

262 rminus of the protein, which adopts an alpha-helical conformation upon lipid binding, is essential fo

263 ation of linear diazido peptides in an alpha-helical conformation upon reaction with dialkynyl linker

264 confirmed that 2 bound to copper in an alpha-helical conformation via its two histidine side chains.

265 hioflavin T, while with SDS, a partial alpha-helical conformation was adopted that gave no fluorescen

266 ion and reconstitution an ~10% loss of alpha-helical conformation was observed, which may reflect the

267 r stabilizing a peptide in a bioactive alpha-helical conformation, we report the discovery of an effi

268 The helical conformations were characterized by X-ray crysta

269 Our results show that SNa15 adopts an alpha-helical conformation when adsorbed to HAP and TiO(2), bu

270 aled that the signal peptide adopted a alpha-helical conformation when bound by NapD, and substitutio

271 The PACAP peptide adopts a helical conformation when bound to hPAC1-R(S) with a ben

272 queous environment, alphaS develops a highly helical conformation when bound to membranes having a ne

273 unstructured in solution, it adopts an alpha-helical conformation when bound to the ECD.

274 argely unstructured in solution but adopts a helical conformation when bound to the GroEL apical doma

275 1-19) is conformationally stable in an alpha-helical conformation when bound to the membrane.

276 bound to the membrane interface in the alpha-helical conformation when the peptide/lipid (P/L) ratios

277 but undergoes a concerted change to an alpha-helical conformation when the polarity of the environmen

278 However, wt-alphaSyn(2SS) adopts an alpha-helical conformation, whereas A30P-alphaSyn(2SS) and A53

279 idues bind the detergent micelle in a partly helical conformation, whereas the remainder of the prote

280 imulations starting with an initial straight helical conformation, whereas the systems with a neutral

281 rminal half of the S4 segment adopts a 3(10)-helical conformation, which appears to be necessary to s

282 cating the initial steps of unfolding of the helical conformation, which are supported by density fun

283 ine II (PPII) and a novel left-handed 2.5(1)-helical conformation, which is an extended beta-strand-l

284 Folding of this peptide into an alpha helical conformation, which occurs upon binding to its t

285 Interestingly, the peptide adopts an alpha-helical conformation, which orients the motif residues t

286 bilayer, alpha-syn takes on a predominantly helical conformation, which spatially separates His50 fr

287 ling preserved the dynamic adoption of alpha-helical conformations, which are essential for physiolog

288 at the N-terminus of alphaS adopts an alpha-helical conformation, while succeeding residues retain t

289 n water, this foldamer adopts a right-handed helical conformation with 3.7 residues per turn, 7.4 A p

290 confirmed that oligomer 8 adopts a two-turn helical conformation with a helical pitch of approximate

291 that both compounds adopt a right-handed 310-helical conformation with both nitronyl nitroxide pendan

292 PrP sequence from residues 89-175 in a beta-helical conformation with the C terminus (residues 176-2

293 it samples polyproline II, beta-strand, and helical conformations with comparable probability.

294 a dynamic equilibria interconverting M and P helical conformations with energetic barriers (DeltaG) o

295 eric form, we found that sarcolipin adopts a helical conformation, with a computed average tilt angle

296 alphaS adopts an extended amphipathic alpha-helical conformation, with its long axis aligned with th

297 n an aqueous environment but adopts an alpha-helical conformation within a localized region on intera

298 re coexists with a broadly distributed ideal helical conformation without interchange on the sub-10 m

299 e groups resulted in disruption of the alpha-helical conformations without loss of water solubility.

300 ss-linking strategy to reinforce their alpha-helical conformation, yielding improved protease resista