ライフサイエンスコーパス: random coil

1 ing (8% alpha-helix, 39% beta-sheet, and 52% random coil).

2 igned to an increase in unordered structure (random coil).

3 structure with D(e) approximately 2 for the random coil.

4 econd fragment tends to remain as a detached random coil.

5 dent of loop size as would be expected for a random coil.

6 ere a highly ordered helix is unraveled to a random coil.

7 nker region between the domains is a dynamic random coil.

8 ing residues retain the characteristics of a random coil.

9 is a structured turn instead of an isotropic random coil.

10 alphaSyn, exhibit a predominant structure of random coil.

11 a trans-trans configuration and behave as a random coil.

12 o approach anything that can be construed as random coil.

13 nd is very different from that expected in a random coil.

14 e polyproline II-like structure instead of a random coil.

15 h the 0.588 predicted for an excluded volume random coil.

16 a beta-strand structure, whereas loop F is a random coil.

17 bility, ranging from local fluctuations to a random coil.

18 melanogaster, which we conclude is a compact random coil.

19 beta-turn and increased the alpha-helix and random coil.

20 owever, the urea-induced DSE deviates from a random coil.

21 isualize the folding pathways initiated from random coils.

22 conformations that are well approximated as random coils.

23 ins include alpha-helices, beta-strands, and random coils.

24 heets starting from random configurations of random coils.

25 distributions align with those of canonical random coils.

26 s that are congruent with those of canonical random coils.

27 parum SSB forms an ensemble of more extended random coils.

28 lled linear macromolecules into "structured" random coils.

29 network (NN) predictions like an increase in random coils.

30 ced assembly/disassembly of the fibrils into random coils.

31 self-avoiding random walks or generic Flory random coils.

32 Do polypeptide chains ever behave like a random coil?

33 AP7 possesses two major sequence regions: a random coil 30-amino acid N-terminal domain (AP7N) and a

34 tive) beta-sheets (55.08%) and alpha-helices/random coils (30.51%), but upon heating from 25 to 95 de

35 (60-80%) in gamma-livetin, and alpha-helices/random coils (60.59%) in alpha-livetin.

36 The functionally relevant random-coil-alpha-helix transition associated with Ca(2+

37 The conversion of the native random coil amyloid beta (Abeta) into amyloid fibers is

38 gnal from tryptophan with an increase in the random coil and alpha helix protein conformations, indic

39 This conformational ensemble is dominated by random coil and bend structures with insignificant prese

40 ucture of the peptide was found to be mainly random coil and beta-strand in the cytoplasm, and possib

41 n between C423 and C453 is populated by both random coil and beta-structure, suggesting that the coop

42 The addition of acid promoted the random coil and beta-turn structures at the expense of a

43 ular beta-sheet structures and a decrease in random coil and beta-turns.

44 an extended conformation consisting of both random coil and heterogeneous beta structures.

45 ssentially all helical, a high percentage of random coil and possibly beta-sheet structure.

46 The lower amount of random coil and triple helix structures allowed higher c

47 The decrease in the random coil and triple helix structures in the gelatin s

48 The lowest amount of random coil and triple helix structures in the interfaci

49 emulsion stability and the lowest amount of random coil and triple helix structures were observed at

50 re-dependent membrane thickness changes: (i) random coiled and bound to the phospholipid head groups

51 ndary structures (alpha-helices, beta-sheet, random coils and turns), as evaluated by FTIR analysis a

52 olated NTD of PR contains a large content of random coil, and it is capable of adopting secondary alp

53 tructure elements (alpha-helix, beta-strand, random coil, and polyproline II), by using the informati

54 nd non-specifically to Abeta, stabilized its random coils, and reduced its cytotoxicity.

55 ices, fibrils, nonfibrillar beta-sheets, and random coils; and four two-phase regions: random coils/n

56 the seven N-terminal residues that are in a random coil as suggested by our analysis of the isolated

57 I are unique to alpha-helix, beta-sheet, and random coil at interfaces.

58 n oligosaccharide and behaves as a stiffened random coil at large molecular mass, in close agreement

59 tration-dependent manner, from predominantly random coil at low surfactant concentration, via beta-st

60 by a sharp conformational transition from a random coil at neutral pH to the more ordered, predomina

61 e-perturbing peptide designed to fold from a random coil at physiological pH to an amphipathic alpha-

62 gregates at low temperatures and disperse as random-coil at high temperatures.

63 Comparison to this random-coil baseline, through secondary chemical shifts,

64 oldable sequences deviate significantly from random coil behavior and that the deviation is fold-depe

65 ly statistically significant deviations from random coil behavior are also evident.

66 yield scaling exponents, nu, consistent with random-coil behavior and yet can also have pockets of re

67 thus, the observed nu(3) is consistent with random-coil behavior.

68 necessary but not sufficient to demonstrate random-coil behavior.

69 by promoting backbone disorder, resulting in random-coil behavior.

70 s of the power-law relationship expected for random-coil behavior.

71 h as R h or R g are very poor indicators of "random coil" behavior.

72 f L18A-L19A-L37A deviates significantly from random-coil behaviour.

73 ) deviated strongly from that expected for a random coil, being in the range -3 to -4.

74 re of the C-terminus was found to be largely random coil, both on the surface of hydroxyapatite as we

75 The stalk regions are predicted to be random coil but contain a variable number of attachment

76 , N(487-503) does not resemble a statistical random coil but instead exists in a loosely structured s

77 te that the unfolded protein is not a simple random coil but rather forms transient structures.

78 unfolded states of globular proteins are not random coils but instead can contain significant amounts

79 he P1 mutant does prefer to be adsorbed as a random coil by approximately 160 kJ/mol, whereas the rev

80 to the theory-predicted shape of a Gaussian random coil chain of nonoverlapping beads, while the str

81 e cytosol and acquires a more beta-sheet and random coil character in the nucleus.

82 ules, the aS structure is still dominated by random-coil characteristics.

83 ative protein ensembles nevertheless exhibit random-coil characteristics.

84 ding residue which are clearly distinct from random coil chemical shift correlations.

85 We estimate the errors in the random coil chemical shift scales to be 0.31 ppm for (13

86 We present a method for calculating accurate random coil chemical shift values of proteins.

87 Deviations from random coil chemical shifts (Delta delta(coil)) indicate

88 backbone amides, and minimal deviations from random-coil chemical shifts for the C-terminal tail of c

89 er than behaving as a homogenous ensemble of random coils, chemical shift changes for the majority of

90 he achiral cyanine dye in association with a random coil CMA, suggesting that the CMA is transformed

91 0.015-0.018 before reaching its steady-state random coil configuration.

92 ture and appears to exist as a collection of random coil configurations.

93 Do highly denatured proteins adopt random coil configurations?

94 flexible polymers that are expected to adopt random-coil configurations, we find that their ion atmos

95 IE, STVIAE, STVIGE, and STVIEE starting from random-coil configurations.

96 tion and are effectively modeled as oriented random coils confined within nuclear boundaries.

97 quivocally indicate that SP1 peptide is in a random coil conformation and mobile in the assembled CA-

98 e full-length peptide, hIAPP 1-19 exhibits a random coil conformation in solution and adopts an alpha

99 uctural transition between alpha-helical and random coil conformation upon changes in pH and ionic co

100 e shielded in aqueous solution by adopting a random coil conformation, enabling the protein to be sol

101 ess than 35 degrees C, this peptide adopts a random coil conformation, rendering it soluble in aqueou

102 heparan sulfate (HS) and presumably adopts a random coil conformation.

103 AF1 appears to come mostly at the expense of random coil conformation.

104 r aggregrates containing peptide segments in random coil conformation.

105 oism spectroscopy revealed a stable, soluble random-coil conformation for amylin in the presence of c

106 sylated and non-glucosylated samples adopt a random-coil conformation in neutral and basic media and

107 view that the linker is endowed with a helix/random coil conformational duality that enables it to be

108 This state is populated by disordered random coil conformations and its lifetime ranges from a

109 h shows that broadly the ensemble of compact random coil conformations can be clustered into four bas

110 ed analogues showed only nascent helices and random coil conformations in H2O.

111 l-lysine in the beta-sheet, alpha-helix, and random coil conformations show that a combination of ami

112 ngate into lower-entropy states (compared to random coil conformations) when crowded, with elongation

113 pts unfolded structure dominated by turn and random coil conformations.

114 dened beta-sheet peak and strong coupling to random coil conformations.

115 bril spectrum distinct from triple helix and random coil conformations.

116 tides showed only nascent helix behavior and random coil conformations.

117 NMR spectroscopy shows that they have mostly random coil conformations.

118 Both folded and random-coil conformations of rat amylin are observed in

119 The structural transition from disordered random-coil conformations to the alpha-extended chain co

120 sulfhydryl content, and Rg, it increased the random coil content, surface hydrophobicity index (Ho),

121 ased, while aggregated beta-sheet, turns and random coil contents increased as temperature increased

122 The alpha-helix and random coil contents of the 600 MPa treated samples were

123 The use of these random-coil data sets rests on the perception that the r

124 t (MW) 547) and fluorophore-labeled flexible random-coil dextran polymers (dex3, MW 3000; dex75, MW 7

125 atures when the particle size approaches the random coil dimensions of the host polymer.

126 esidues in the N-terminal subdomain sample a random-coil distribution of conformations, deviations of

127 h a transition from double stranded helix to random coil DNA.

128 artificial alpha-helical leucine zipper and random coil domains fused to a polyphenol oxidase, small

129 lysis of P2 showed largely alpha-helical and random coil domains.

130 our well-defined beta-sheet regions and four random-coil elements with varying degrees of local dynam

131 coincide with the dimensions predicted for a random coil ensemble, potentially statistically signific

132 istinguishable from the mean dimensions of a random-coil ensemble.

133 es, and this feature implies a selection for random coil ensembles.

134 mean radii of gyration that agree well with random-coil expectations in all but two cases.

135 ions: random coils/nonfibrillar beta-sheets, random coils/fibrils, fibrils/nonfibrillar beta-sheets,

136 , bends, alpha-helices, beta-structures, and random coils for inactivated viruses compared with the M

137 ollowed by a non-cooperative transition to a random-coil form as more guanidine is added.

138 nts by CD spectroscopy indicated significant random-coil formation in G473D, G473W, and R212A/G473D.

139 The random-coil fraction of the protein increased after reti

140 pectroscopy showed changes in structure from random coil --> alpha-helix --> beta-sheet, with increas

141 All peptides displayed a random coil --> alpha/beta --> beta transition, but subs

142 nd the structure of the nucleic acids (e.g., random coil, hairpin, or duplex).

143 The Gaussian-distributed random coil has been the dominant model for denatured pr

144 melt directly from the solid state to become random coils, helices, and turns.

145 A random coil-helix transition underlies the association o

146 mer is shown to be and to behave more like a random coil homopolymer, after passing through a 250 kg

147 ation of the basket-type G-quadruplex from a random coil human telomeric oligonucleotide, even in the

148 the literature, GLP-1 has been shown to be a random coil in free solution, adopting a folded, alpha-h

149 The transition from a random coil in solution to a folded state in a membrane

150 re with Fe(3+)-PPIX binding, changing from a random coil in the absence of Fe(3+)-PPIX to a more orde

151 e of 8% alpha-helix, 45% beta-sheet, and 48% random coil in the C-terminal peptide with noticeable st

152 n a region of the molecule known to exist as random coil in the lipid-free state.

153 ns of amelogenin that appear to be primarily random coil in the nanosphere-gel adopt a beta-strand st

154 central linker from predominantly helical to random coil in this temperature range.

155 ltiple independent techniques to behave as a random coil in water, suggesting that it is unlikely to

156 ational ensemble of the domain deviates from random coil, in agreement with previous findings from NM

157 reased, but aggregated beta-sheet, turns and random coil increased.

158 erception is stunted in samples containing a random coil, ionic, mucoadhesive thickener, the retentio

159 nt that a scaling exponent consistent with a random coil is necessary but not sufficient to demonstra

160 indicate that FG repeats are highly dynamic random coils, lack intrachain interactions, and exhibit

161 Phosphorylation makes the CTD more like a random coil leaving open the question of how Src exerts

162 he overall structure of the hIAPP peptide is random coil-like and lacks a dominant folded structure.

163 ydrodynamic radius that is consistent with a random coil-like polypeptide.

164 corresponding to an increased population of random coil-like structures with weak hydrophobic and el

165 ied, and oligomerization does not change the random-coil-like conformation observed.

166 fectively an ensemble of protein chains with random-coil-like conformations.

167 o the backbone and induces a transition to a random-coil-like structure.

168 endent evidence have raised doubts about the random coil model and offer support for alternative view

169 This result is inconsistent with a random coil model and the general view that these peptid

170 However, the random-coil model is specified by the global geometric p

171 l space is over-estimated by the traditional random-coil model, in which local steric restrictions ar

172 conformations, in apparent conflict with the random-coil model.

173 hifts indicate the completely unstructured, "random coil" model for elastin is unlikely.

174 (15)N R2 relaxation rates deviate from random coil models, suggesting hydrophobic clustering in

175 g earlier, scattering-based evidence for the random coil nature of the unfolded state with more site-

176 The random-coil nature of zeta(cyt) was also confirmed by he

177 One such use is as a baseline for random-coil NMR chemical shifts.

178 nd random coils; and four two-phase regions: random coils/nonfibrillar beta-sheets, random coils/fibr

179 The random coils of IGSII and IVIGS showed no tendency to as

180 established a mechanism for the folding of a random coil oligo into the iM.

181 ize the helix conformation over the "native" random coil ones for in silico designed model peptides.

182 playing a turn motif from 1 to 22.5 ns and a random coil pattern from 22.5 to 50 ns.

183 at TAT(48-60) is a highly dynamic and nearly random coil peptide in the lipid bilayer and inserts int

184 We find that, at a low concentration, random-coil peptides assemble into alpha-helices at low

185 At intermediate concentrations, random-coil peptides assemble into alpha-helices at low

186 d the log of the loop size is expected for a random coil, pK(a)(obs) proportional to k log(n), where

187 core thickness that scales for large MW as a random coil polymer, in agreement with experiment.

188 ble with a model that treats the linker as a random-coil polymer.

189 are known to be important in the dynamics of random coil polymers and colloids.

190 natured chain, which obeys the statistics of random coil polymers.

191 of the protein between globular proteins and random coil polymers.

192 It is generally held that random-coil polypeptide chains undergo a barrier-less co

193 folding-competent states, as compared with a random-coil polypeptide, may contribute to the slow in v

194 les predicted by a computational model for a random-coil polypeptide.

195 -reduced form, A4V apoSOD1 exchanged like a "random coil" polypeptide at 20 degrees C and began to po

196 es, the peptide exists mostly as a collapsed random coil, populating a small fraction (less than 10%)

197 ease in the intensity of resonances near the random coil positions is characterized by a similar time

198 ide variants and deviates significantly from random coil predictions for both NMR and SAXS data.

199 crease in nucleic acid and beta-sheet and/or random coil protein content along with a decrease in alp

200 This is in direct contrast with the random coil protein PEVK of titin, which readily extends

201 uencing by capillary electrophoresis using a random-coil protein drag-tag of unprecedented length and

202 Importantly, the predominance of the random coil provides plasticity for the formation of fun

203 its amide hydrogens with water hydrogens at random coil rates, consistent with its natively unstruct

204 ructural changes that occur upon addition of random coil (RC) monomer fragments from the yeast prion

205 conformation for both peptides resulted in a random coil (RC) structure, with the helix (H) conformat

206 By comparison with a random coil reference state, the nascent structure in th

207 The random-coil region is at high temperatures and all conce

208 Random coil residues are also observed, which do not the

209 alpha), and (13)C(beta) chemical shifts from random coil reveals that there are four regions between

210 y denatured state for a variety of proteins, random coil scaling of the radius of gyration and the pr

211 es contain a large amount of alpha-helix and random coil secondary structure as measured by circular

212 s detected here have either alpha-helical or random coil secondary structure, depending on solvent an

213 egation despite that both conformers possess random coil secondary structures indistinguishable from

214 hyl resonance of Ile556, located in a short, random coil segment following helix E, experiences a lar

215 thought to be an intrinsically unstructured random-coil segment.

216 We reveal that the short variable N-terminal random coil sequences of STIM1 and STIM2 confer profound

217 Cylindrical, helical, and random coil shape models were fitted to the SANS measure

218 The PEVK domain of titin encodes a random coil shown to be an important factor in the passi

219 y of ligand binding above that achieved by a random-coil ssRNA.

220 ecifically recognize the epitope region in a random coil state.

221 of the peptide to a greater extent than the random coil state.

222 alpha-helical conformation to a beta and/or random coil state.

223 In addition to its random-coil state, alpha-syn can adopt an alpha-helical

224 tructure, leaving the remainder in a mobile, random-coil state.

225 s and all concentrations, the system is in a random-coil state.

226 -helical state toward the inactive, unbound, random-coil state.

227 etailed view of conformations making up the "random coil" state.

228 mations diminishes in favor of beta-turn and random-coil states.

229 ions that are more extended than the typical random-coil states.

230 We see no evidence of any disordered "random coil" states.

231 e unusually compact, strongly deviating from random coil statistics.

232 ved that unfolded or denatured proteins show random-coil statistics and hence their radius of gyratio

233 nstrated that highly denatured proteins obey random-coil statistics.

234 n contrast, an increase in alpha-helical and random coil structural components relative to the normal

235 EPS2 was found to adopt a random coil structural conformation.

236 portions of extended beta strand relative to random coil structure and sequence spacing of Asp, Glu r

237 transform infrared (FT-IR) spectra revealed random coil structure in OD-FPH and beta-sheet in FD-FPH

238 The random coil structure of TAT and another CPP, penetratin

239 The CTD-Rtt103 association opens the compact random coil structure of the CTD, leading to a beads-on-

240 5I26L27 region of hIAPP, which starts from a random coil structure, evolves into ordered beta-sheet o

241 e in helical content and formation of a more random coil structure, resulting in protein unfolding, i

242 nd also possesses significant beta-sheet and random coil structure.

243 monomer hairpin followed by conversion to a random coil structure; whereas at high salt concentratio

244 cular dichroism on the same samples showed a random-coil structure and no oligomers.

245 e stable, whereas at higher temperatures the random-coil structure predominates.

246 riods of incubation dissociates readily into random-coil structure upon dilution into Tris buffer.

247 ile amelogenin nanospheres had predominantly random-coil structure.

248 linker by insertion of nine amino acids of a random-coiled structure uncoupled the ECD from regulatin

249 The computed preference for random coil structures is in agreement with NMR experime

250 between the fits of the query structures and random coil structures to these experimental data.

251 eigenstates much more than already exists in random coil structures.

252 whereas in water they adopt largely compact random coil structures.

253 The "linear lattice" model proposed random-coil structures for both normal and expanded poly

254 and Abeta42 are peptides that adopt similar random-coil structures in solution.

255 e misfolding of hIAPP from alpha-helical and random-coil structures to the parallel beta-sheet struct

256 for NMIIA filament disassembly: Part of the random coil tailpiece and the C-terminal residues of the

257 ActA is a natively unfolded protein, largely random coil that is responsible for many of the unique p

258 > or = 1.5 mM Mg(2+) leads to an ensemble of random coils that fold with multistage kinetics.

259 s well-described as a denaturant-independent random coil, this similarity raises questions regarding

260 drives a T(33) conformational change from a random coil to a folded structure.

261 bly continuous) structural transition from a random coil to a globular conformation on reducing the t

262 The polymorphous TL must convert from a random coil to a helical hairpin that contacts the nucle

263 ealed that a 29mer SPA peptide shifts from a random coil to a helix in a concentration-dependent mann

264 cture as a result of phosphorylation, from a random coil to a largely helical structure, and V(19)L(2

265 major conformational changes, from a relaxed random coil to a stretched configuration, following a un

266 etry indicated that peptide TZ1H undergoes a random coil to alpha-helical conformational change upon

267 6-146, and 179-236) change conformation from random coil to alpha-helix so that nearly the entire apo

268 4 to the lipid membrane is associated with a random coil to alpha-helix structural transition.

269 t prion-like protein Sup35 by simulating the random coil to beta-sheet and alpha-helix to beta-sheet

270 de exhibits a conformational transition from random coil to beta-sheet by changing the pH from acidic

271 o cause a conformational change from compact random coil to extended helical structure-the disappeara

272 ically, alphaS undergoes a transition from a random coil to helical conformation upon encountering sy

273 m the Listeria protein ActA that undergoes a random coil to helix transition upon lipid binding.

274 ring the entire fibrillogenesis process from random coil to mature fibrils, including the molecular s

275 eptides invariably collapse from an expanded random coil to more compact dimensions as the denaturant

276 duced a conformational change from a relaxed random coil to more intricate secondary structures (e.g.

277 protein structure that is initially rich in random coil to one that is rich in beta-sheet content.

278 l-length apoE single Cys variants, a similar random coil to stable backbone transition was observed,

279 nd in real time the misfolding of hIAPP from random coils to alpha-helices and then beta-sheets upon

280 suggests that it transforms from disordered (random coil) to alpha helical structure.

281 A random coil-to-helix transition mechanism has now been i

282 E) has been used to characterize the hairpin-random coil transition of four octamers in the GCxxxxGC

283 on has been proposed to result in a helix to random-coil transition.

284 , indicative of a well-solvated and expanded random coil under all of the conditions examined.

285 rotein achieves its native conformation from random coil under physiologically relevant conditions re

286 ns can be envisioned as the contraction of a random coil unfolded state toward the native state on an

287 chemical shift values that are very close to random coil values and indistinguishable between the two

288 f the deviations of the chemical shifts from random coil values indicates that residues that comprise

289 de 1H and 15N chemical shifts from canonical random-coil values for residues within 5A of the His41 i

290 d comparing the chemical shifts to published random-coil values, and by measuring (1)H-(15)N heteronu

291 markers are identified that uniquely monitor random coil versus beta-sheet secondary structures as we

292 the protein chain is expected to behave as a random coil, where the H residues are "wrapped" locally

293 mers of both variants exist predominantly as random coils, whereas the oligomers form predominantly b

294 y rationalized using a simplified model of a random coil whose two ends must be a specific distance a

295 CLK2-PAGE4 is more expanded and resembles a random coil with diminished affinity for AP-1.

296 find that polyalanine closely approximates a random coil with excluded volume giving scaling exponent

297 0, close to the value of -2.2 expected for a random coil with excluded volume.

298 cture, consisting mostly of beta-strands and random coil with two small alpha-helices.

299 peptide mainly consisted of beta-strands and random coils with unfolded structure.

300 In contrast, the HVR is overwhelmingly a random coil, with the structured alpha-helices and beta-