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

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

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

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

7 elf and from cellulose and expands to form a random coil.

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

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

10 ing residues retain the characteristics of a random coil.

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

12 alphaSyn, exhibit a predominant structure of random coil.

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

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

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

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

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

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

19 isualize the folding pathways initiated from random coils.

20 conformations that are well approximated as random coils.

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

22 heets starting from random configurations of random coils.

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

24 distributions align with those of canonical random coils.

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

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

27 lled linear macromolecules into "structured" random coils.

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

29 Do polypeptide chains ever behave like a random coil?

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

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

32 (60-80%) in gamma-livetin, and alpha-helices/random coils (60.59%) in alpha-livetin.

33 A higher proportion of beta sheets, random coils, alpha-helix and beta-turns for all fractio

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

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

36 oscopy in vitro displays the properties of a random coil and acts as an entropic spring.

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

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

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

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

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

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

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

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

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

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

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

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

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

50 ices, and an increase in aggregated strands, random coils and aromatic side chains in the muscle fibr

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

83 The assignment of all (1)H, (13)C and (15)N random coil chemical shifts of pGlu in short reference p

84 mical shift pairs that are distinct from the random coil chemical shifts of the natural amino-acid re

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

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

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

88 0.015-0.018 before reaching its steady-state random coil configuration.

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

90 Do highly denatured proteins adopt random coil configurations?

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

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

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

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

95 toughness originating from their alpha-helix/random coil conformation structures and their micro-fibr

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

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

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

99 r aggregrates containing peptide segments in random coil conformation.

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

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

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

103 Sec63 unit of Brr2 (Brr2(C-Sec63)), adopt a random-coil conformation in their unbound state.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

127 oriented molecular chains tend to revert to random coils during aging.

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

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

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

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

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

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

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

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

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

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

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

139 s further and noted a partial unfolding of a random-coil helix within the region 531-537 in the apo s

140 A random coil-helix transition underlies the association o

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

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

143 the wild type state (q=+8) is essentially a random coil, hyper-acetylated H4 (q=+3) is virtually as

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

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

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

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

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

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

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

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

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

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

154 It compares random coil index [RCI] against local rigidity predicted

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

171 tates are consistent with those of canonical random coils, namely polymers in indifferent (theta) sol

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

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

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

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

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

177 splay chemical shifts that are indicative of random coil or beta-sheet conformations.

178 entropy and hydrophobic interaction favoring random coil or globular states, respectively.

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

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

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

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

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

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

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

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

187 simulation and theory to show that flexible random-coil polymers bind more strongly than stiff rod-l

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

189 defined-length, N-terminal Pro/Ala/Ser (PAS) random-coil polypeptide with IL-1Ra.

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

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

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

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

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

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

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

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

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

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

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

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

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

203 emble-averaged properties, characteristic of random coils (RCs), the conformational ensembles of the

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

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

206 lical segments, beta-sheets, beta-turns, and random coil regions were less stable than in C(H)2s and

207 d dimer interface and an increased number of random-coiled regions, suggesting that a general loss in

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

238 5I26L27 region of hIAPP, which starts from a random coil structure, evolves into ordered beta-sheet o

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

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

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

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

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

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

245 ile amelogenin nanospheres had predominantly random-coil structure.

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

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

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

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

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

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

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

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

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

255 a CD spectrum consistent with features of a random coil, the protein is correctly folded as indicate

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

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

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

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

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

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

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

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

264 6-146, and 179-236) change conformation from random coil to alpha-helix so that nearly the entire apo

265 4 to the lipid membrane is associated with a random coil to alpha-helix structural transition.

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

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

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

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

270 exhibited faster conformational changes from random coil to its beta-sheet fibrillar states.

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

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

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

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

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

276 amely the folding of antigenic peptides from random coils to alpha-helical structure, is important fo

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

278 pSs) and a shift in secondary structure from random coils to beta-structures, creating infrared spect

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

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

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

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

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

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

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

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

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

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

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

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

291 l component analysis identified variation in random coil, water content, lipid carbonyl and methylene

292 asic and SP-rich domains are predicted to be random coil, whereas the segments S111-I116, A124-R132,

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

294 water fraction comprised of alpha-helix and random coils, while salt and alkali fractions contained

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

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

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

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-