ライフサイエンスコーパス: folding intermediate

1 ucture and the generation of the three-helix folding intermediate.

2 is determined by the dynamic population of a folding intermediate.

3 c stability, and thus the population, of the folding intermediate.

4 B/helix C packing interactions occur in the folding intermediate.

5 non-native contacts in stabilization of the folding intermediate.

6 w folding forms also takes place in an early folding intermediate.

7 lateaus, suggesting the presence of a stable folding intermediate.

8 E3 and apoE2 and more prone to form a stable folding intermediate.

9 re often taken as a sign for a thermodynamic folding intermediate.

10 ular dichroism, suggesting the presence of a folding intermediate.

11 alpha subunit was less tightly packed in the folding intermediate.

12 and volumetric properties of the on-pathway folding intermediate.

13 an excellent model for an obligatory kinetic folding intermediate.

14 state kinetics without the accumulation of a folding intermediate.

15 arnase is inconsistent with the absence of a folding intermediate.

16 estigated as a model of an oxidative protein-folding intermediate.

17 rface, but is not a classical molten-globule folding intermediate.

18 and another of which we have identified as a folding intermediate.

19 e latter, that may correspond to a transient folding intermediate.

20 non-two-state folding for insulin through a folding intermediate.

21 folded-state structure, and a putative early folding intermediate.

22 arge amounts of a nonfunctional N1922S-fVIII-folding intermediate.

23 intron (aI5gamma) primarily by stabilizing a folding intermediate.

24 bes specific interactions in the core of the folding intermediate.

25 resolve closely spaced, transiently occupied folding intermediates.

26 s process due to the difficulty in detecting folding intermediates.

27 facilitates the identification of pseudoknot folding intermediates.

28 abeling method for determining structures of folding intermediates.

29 tions are good structural models for kinetic folding intermediates.

30 ion while avoiding destruction of productive folding intermediates.

31 ct as an RNA chaperone or by stabilizing RNA folding intermediates.

32 , they contribute little to the stability of folding intermediates.

33 ive stabilities of the dimeric and monomeric folding intermediates.

34 g arm and bends in the unfolding arm suggest folding intermediates.

35 may exhibit a similar, signature pattern of folding intermediates.

36 ng the absence of detectable sub-millisecond folding intermediates.

37 ficiency reveals two previously undetermined folding intermediates.

38 s with the appearance of prophase chromosome folding intermediates.

39 roach for visualizing RNA folding states and folding intermediates.

40 determining the high-resolution structure of folding intermediates.

41 o slow folding and cause the accumulation of folding intermediates.

42 ding of barnase that involves two detectable folding intermediates.

43 ral and kinetic analysis of the acid-trapped folding intermediates.

44 se partial folds provide models of oxidative folding intermediates.

45 ons is not conclusive proof of thermodynamic folding intermediates.

46 he ER and ERGIC/CGN recognize distinct furin folding intermediates.

47 in the absence of the accumulation of early folding intermediates.

48 in order to trap and characterize different folding intermediates.

49 seful tools for the characterization of LamB folding intermediates.

50 ructural and energetic properties of kinetic folding intermediates.

51 d to the enhanced stability of the transient folding intermediates.

52 asing the concentration of aggregation-prone folding intermediates.

53 ing structured populations in conformational folding intermediates.

54 hat mis-folded species are formed from early folding intermediates.

55 ble details on the structures of equilibrium folding intermediates.

56 We then predict thermodynamic folding intermediates.

57 utes a novel type of evidence for on-pathway folding intermediates.

58 ral and kinetic analysis of the acid-trapped folding intermediates.

59 novel structural information on equilibrium folding intermediates.

60 high affinity to early unstructured protein folding intermediates.

61 presence of 3-disulfide scrambled isomers as folding intermediates.

62 e hybridization facilitates the detection of folding intermediates.

63 ctive structure relative to compact inactive folding intermediates.

64 many other proteins populate molten globule folding intermediates.

65 would favor aggregation of unstable protein folding intermediates.

66 imerization proceeded through multiple, slow-folding intermediates.

67 own to progress through disulfide-bonded Vp1 folding intermediates.

68 estrated by PQC through the interaction with folding intermediates.

69 mediate Hsp33's high affinity for structured folding intermediates.

70 binding and stabilizing met-alpha hemichrome folding intermediates.

71 te between unfolded and partially structured folding intermediates.

72 at allows direct analysis of cotranslational folding intermediates.

73 nts </=1), and are associated with populated folding intermediates.

74 eneity and diverse rearrangement pathways of folding intermediates.

75 role in the stabilization of group II intron folding intermediates.

76 with human beta-actin or yeast ACT1p protein folding intermediates, Ac(I), pre-synthesised in an Esch

77 We conclude that RNA folding intermediates adopt extended conformations due t

78 mer thus represents a compact but metastable folding intermediate along the pathway to assembly of th

79 -termini make physical contact with the PepQ folding intermediate and help retain it deep within the

80 city and malleability of core packing in the folding intermediate and rate-limiting transition state.

81 ydrogen exchange methods identifies a second folding intermediate and reveals the order and free ener

82 eas a large barrier exists between the major folding intermediate and the denatured states.

83 in binding reveals an antagonism between the folding intermediate and the full native structure.

84 ical structure in the F helix of the kinetic folding intermediate and to increase its propensity to f

85 Obtaining detailed knowledge of folding intermediate and transition state (TS) structure

86 e they are formed, but it could capture some folding intermediates and activate them, even though the

87 pportunity to determine the structure of RNA folding intermediates and conformational trajectories.

88 esolution structural information about early folding intermediates and denatured states under conditi

89 developed to probe the dynamic structure of folding intermediates and folded complexes of proteins u

90 g higher order RNA structure, especially for folding intermediates and for RNAs whose functions requi

91 interactions between glycerol-induced PmMDH folding intermediates and GroEL.GroES.ATP are diminished

92 n a reversible equilibrium between monomeric folding intermediates and higher-order oligomers.

93 h extracts crucial information about protein folding intermediates and mechanism.

94 on properties of proteins, and for detecting folding intermediates and other structural details of pr

95 detection of information relating to protein folding intermediates and pathways can be monitored by l

96 netic, and thermodynamic information for the folding intermediates and pathways of many proteins is c

97 ical for understanding the nature of protein-folding intermediates and protein-folding pathways, prot

98 hibit both a high degree of heterogeneity of folding intermediates and the accumulation of scrambled

99 transition determines the structures of the folding intermediates and the folding time to the native

100 y can now determine the structure of protein folding intermediates and their progression in folding p

101 However, direct structural information on folding intermediates and their properties now indicates

102 tructural relationship between these gaseous folding intermediates and those in solution is apparent,

103 experimental data revealed the structures of folding intermediates and transition states and their as

104 Protein folding intermediates and transition states are commonly

105 lues and Hammond-type behaviors exhibited by folding intermediates and transition states may arise mo

106 non-native structures of proteins that mimic folding intermediates and/or conformations that occur in

107 influenced more heavily by specific membrane folding intermediates, and as a result yield different p

108 GroEL can capture early folding intermediates, and it loses the ability to captu

109 he formation of stable Tel22 G-quadruplexes, folding intermediates, and ligand-quadruplex complexes,

110 led conformational heterogeneity, metastable folding intermediates, and long-lived states with distin

111 hod is used here to characterize some of the folding intermediates, and the oxidative folding process

112 otifs is cooperatively linked in near-native folding intermediates, and this cooperativity depends on

113 Questions such as whether there are genuine folding intermediates, and whether the events at the ear

114 At pH 4.0, a pH value known to stabilize folding intermediates, apoE4 and apoE3 displayed the sam

115 pite an exceedingly large number of possible folding intermediates ( approximately 46 million disulfi

116 The 3D models for the HIV-2 RRE and folding intermediates are also presented, wherein the Re

117 structures of protein native states and some folding intermediates are available, the mechanism of in

118 he thermodynamic states corresponding to the folding intermediates are better conserved than their st

119 In general, these folding intermediates are considerably less compact than

120 efficiency whereby quasinative alpha-tubulin folding intermediates are generated via ATP-dependent in

121 X NMR was used to show that the PUFs and the folding intermediates are likely the same species.

122 Two folding intermediates are observed, the second of which

123 Protein folding intermediates are often imperative for overall f

124 es has been characterized, the structures of folding intermediates are poorly defined.

125 a particularly challenging problem, because folding intermediates are predicted to be unstable in ei

126 vide the first direct evidence that multiple folding intermediates are present in solution.

127 why the prodomain is needed to stabilize the folding intermediate as well as why the unfolding of fre

128 d efficiency in the generation of productive folding intermediates as a result of inefficient interac

129 to constrain coarse-grained models of these folding intermediates as we investigate the role of nonn

130 trations of urea shows a low population of a folding intermediate, as inferred from an intensity-base

131 n all assays correlated with the presence of folding intermediates, as observed with urea denaturatio

132 The structure of the apoE4 folding intermediate at pH 4.0 in 3.75 m urea was charac

133 t the structure of infinitesimally populated folding intermediates at equilibrium and kinetic interme

134 he varied extent of (a) the heterogeneity of folding intermediates, (b) the predominance of intermedi

135 nd no evidence for the existence of a stable folding intermediate before the rate-limiting transition

136 The collapsed RuBisCO folding intermediate binds to the lower segment of two a

137 In contrast, none of the folding intermediates bound to PAI-1 or to mAb 153.

138 the nucleus centered on helix(1) formed in a folding intermediate but also show the efficacy of this

139 x of how Hsp90 specifically selects for late folding intermediates but also for some intrinsically di

140 ike for cytochrome c, there is an observable folding intermediate, but no microsecond burst phase in

141 between the native state and a well-defined folding intermediate by about 20-fold, under conditions

142 We stabilized this hypothetical folding intermediate by deleting a residue (P174) in the

143 In 1971 we began to search for protein folding intermediates by fast-reaction methods.

144 bsence of detectable kinetic and equilibrium folding intermediates by optical probes is commonly take

145 nosylation of un-/misfolded proteins or slow folding intermediates by Pmt1-Pmt2 complexes.

146 e structure of the folded region of an early folding intermediate can be as well defined as the nativ

147 stage, formation of helices II and III as a folding intermediate constituted the rate-limiting step

148 ne knot disulfide bonds resulted in multiple folding intermediates containing 1, 2, or 4 disulfide bo

149 nteractions, immunoglobulin (Ig) heavy chain folding intermediates containing bound GRP94 and immunog

150 that of BPTI, exhibiting limited species of folding intermediates containing mostly native disulfide

151 de-loaded MHC class I complexes as it did to folding intermediates created in vitro, namely free clas

152 n of intracellular and secreted forms of the folding intermediates demonstrated that the most folded

153 a result of the association of two monomeric folding intermediates, demonstrating that procaspase-3 d

154 haperones, termed cofactors A-E, that act on folding intermediates downstream of the cytosolic chaper

155 ty of partial aggregation caused by the slow folding intermediates during its spontaneous refolding p

156 cteriorhodopsin has to populate at least two folding intermediates, during folding in the mixed lipid

157 eliminated, the thermodynamic signature of a folding intermediate emerges, and a marked decrease in f

158 measurement, it is possible to determine the folding intermediates, energies, and kinetics of the mac

159 Although most folding intermediates escape detection, their characteri

160 6), as well as very fast folding proteins or folding intermediates estimated to lie near the speed li

161 stingly, phi influences the stability of the folding intermediates (FI(1) and FI(2)) in an apparently

162 recently have determined the structure of a folding intermediate for a four-helix bundle protein (Rd

163 ies, in the presence of additional monomeric folding intermediates for alphaTS and sIGPS and in rate-

164 de reduction-reoxidation may set up critical folding intermediates for intramolecular isomerization,

165 to stabilize the hydrogen-bonded networks in folding intermediates for other TIM barrel proteins, it

166 used to explore the structure of the stable folding intermediates for the of indole-3-glycerol phosp

167 , we also solved the structures of two other folding intermediates for the same protein: one with the

168 ns in the early secretory pathway yet spares folding intermediates from being destroyed.

169 lex that acts as a guardian to protect these folding intermediates from being targeted for ERAD.

170 to ribosomes and protects nascent chains and folding intermediates from nonproductive interactions.

171 ve the conformations and energies of protein folding intermediates from single-molecule manipulation

172 The folding intermediate further acted as a template that fa

173 While the transition states and folding intermediate have been characterised in atomisti

174 Folding intermediates have been detected and characteriz

175 energy between native actin and a non-native folding intermediate (I(3)) is characteristic of a parti

176 e heterogeneity and extensive overlapping of folding intermediates, identification of the predominant

177 and fluorescence suggested the presence of a folding intermediate in apoE, most prominently in apoE4.

178 the same native state, transition state, and folding intermediate in both simulation systems, and was

179 the isolation and purification of a protein folding intermediate in native condition.

180 We see evidence for a well defined folding intermediate in the acid renaturation folding pa

181 modeling indicates that the stability of the folding intermediate in water is only 1.5 kcal/mol.

182 strategy to ubiquitin, reversibly trapping a folding intermediate in which the beta5-strand is unfold

183 4 the native protein forms a molten globule folding intermediate in which the histidine residues are

184 to the experimentally determined equilibrium folding intermediates in a set of nine proteins.

185 ings may provide an understanding of protein folding intermediates in general and lead to a procedure

186 athway oligomers, allowing us to study early folding intermediates in isolation from higher-order spe

187 with nascent tertiary interactions, compact folding intermediates in RNA also play a crucial role in

188 The structural characterization of oxidative folding intermediates in terms of disulfide pairing is d

189 Potential folding intermediates in the formation of the microflore

190 ral heptad repeat peptides that bind only to folding intermediates in the S-mediated fusion process a

191 al transitions, thereby protecting transient folding intermediates in vivo that could contribute to p

192 playing a highly heterogeneous population of folding intermediates, including fully oxidized scramble

193 refolded faster than FKBP(*) but lacked the folding intermediate, indicating that these mutants expe

194 om these studies, we conclude that the apoE4 folding intermediate is a single molecule with the chara

195 The potential functional significance of the folding intermediate is discussed.

196 approach can be used to establish whether a folding intermediate is on-pathway or off-pathway.

197 titration experiments indicate that a stable folding intermediate is present at stoichiometric concen

198 Initial collapse to off-pathway folding intermediates is a common feature of the folding

199 idation of the high-resolution structures of folding intermediates is a necessary but difficult step

200 The formation of productive folding intermediates is further hindered by the topolog

201 The characterization of early folding intermediates is key to understanding the protei

202 in highly populated and the concentration of folding intermediates is low.

203 he location of the GroEL binding site on the folding intermediate, mapped from (15)N, (1)HN, and (13)

204 sis that the structured regions in a protein folding intermediate may correspond to regions that can

205 An early mCG-beta folding intermediate, mpbeta1, contained two disulfide b

206 The subsequent folding intermediate, mpbeta2-early, was represented by

207 n of KCl led to the formation of a transient folding intermediate not observed at lower salt concentr

208 ermine an atomic resolution structure of the folding intermediate of a small protein module--the FF d

209 We demonstrate that a folding intermediate of AML1-ETO binds to TRiC directly,

210 ctron microscopy, we demonstrate here that a folding intermediate of AML1-ETO's DNA-binding domain (A

211 cture in both the burst-phase molten globule-folding intermediate of apomyoglobin and in an equilibri

212 otherwise apparently homogeneous equilibrium folding intermediate of Borrelia burgdorferi OspA into t

213 ent conformational ensemble of a burst-phase folding intermediate of disulfide-intact RNase A.

214 Our calculations reveal the existence of a folding intermediate of GB3 with nonnative structural el

215 The major folding intermediate of hen egg-white lysozyme has a coo

216 r data suggest that pentamidine binding to a folding intermediate of hERG arrests channel maturation

217 ined Phi-values, we show that the on-pathway folding intermediate of Im7 contains extensive, stable h

218 Our data show that Hep1 bound to a folding intermediate of mtHsp70.

219 y reported backbone amide protection for the folding intermediate of N-PGK.

220 Hsc70 and Ydj1 can trap an import-competent folding intermediate of pmAAT, but productive binding an

221 in interactions, the structure of the hidden folding intermediate of T4 lysozyme is largely native-li

222 on structural and dynamic features within a folding intermediate of the amyloidogenic protein beta2-

223 istidine residues of an invisible on-pathway folding intermediate of the colicin E7 immunity protein.

224 vel model of a highly structured equilibrium folding intermediate of the specificity domain of the Ba

225 rected protein engineering, we populated the folding intermediate of the Thermus thermophilus ribonuc

226 2.2 A from wild-type VEGF, identifies a true folding intermediate of VEGF.

227 entify cotranslational and posttranslational folding intermediates of a periplasmic protein in which

228 tion to monitor progression of intracellular folding intermediates of a previously uncharacterized pr

229 In the presence of calcium, the folding intermediates of alpha LA comprise two predomina

230 he changes in the conformational dynamics in folding intermediates of proteins that contain only a su

231 c HSP proteins are sequentially recruited to folding intermediates of the A2A receptor.

232 the cysteine sidechain thiols in the kinetic folding intermediates of the N-terminal domain of phosph

233 ning ribozyme provides insight into possible folding intermediates of the ribozyme.

234 Unlike the folding intermediates of the two single-domain proteins,

235 these conditions, even the earliest tertiary folding intermediates of the wild-type ribozyme represen

236 We find that crowding does not introduce new folding intermediates or misfolded structures, although,

237 doknotted structures are allowed to occur as folding intermediates or not.

238 tails of the folding pathways such as stable folding intermediates or the timing of the folding proce

239 nt misligated Co(III) species, and, as these folding intermediates persist for several hours under ce

240 The denatured state is a well-ordered folding intermediate, poised to fold by docking helices

241 ort a folding mechanism wherein at least one folding intermediate populates behind the main rate-limi

242 ity of AHSP to stabilize nascent alpha chain folding intermediates prior to hemin reduction and incor

243 The knowledge of the structure for the ApoE4 folding intermediate provides a new platform for the rat

244 mediate, and unfolded) showed that the apoE4 folding intermediate reached its maximal concentration (

245 of pressure, which favors the population of folding intermediates relative to chemical denaturants;

246 ze that the presence of a long-lived protein folding intermediate renders a protein sensitive to Skp.

247 e find that progression to this second early folding intermediate requires RNA sequence motifs that e

248 The low stability of nascent folding intermediates results in part from subtilisin's

249 The folding intermediates revealed that rhm-CSFbeta folds sy

250 lded slightly faster and exhibited a kinetic folding intermediate similar to that of FKBP(*).

251 he experimentally detected aggregation-prone folding intermediate species of monomeric native gammaD-

252 The native state is separated from the major folding intermediate state by a small barrier, whereas a

253 Here, we investigated the equilibrium (un)folding intermediate state of T4 phage gene product 45 (

254 fined unfolding is a common feature of early folding intermediate states and accounts for why there a

255 and quantify conformational heterogeneity of folding intermediate states.

256 ive distributions of hybrid-1, hybrid-2, and folding intermediates such as triplexes.

257 Hsp90 and its co-chaperones as an on-pathway folding intermediate, suggesting that Delta508 CF diseas

258 his system revealed that three-stranded gp41 folding intermediates susceptible to the inhibitor enfuv

259 e structures tend to have more pseudoknotted folding intermediates than RNAs with pseudoknot-free gro

260 action involves the formation of an unstable folding intermediate that is captured by the binding of

261 alled Lyso-alpha, as a model of the lysozyme folding intermediate that is stable at equilibrium.

262 etween the native heterodimeric enzyme and a folding intermediate that is well-populated in 2 M urea.

263 mediate state corresponded closely to a late-folding intermediate that we detected in time-resolved s

264 The monomeric and dimeric folding intermediates that appear during the folding rea

265 these species represent kinetically distinct folding intermediates that are not identical as previous

266 RNA, such as a nick in P9, populate kinetic folding intermediates that are not observed in the natur

267 to a population of destabilized, off-pathway folding intermediates that are toxic to motor neurons.

268 we show that UCH-L1 has two distinct kinetic folding intermediates that are transiently populated on

269 feature may be the formation of off-pathway folding intermediates that are unstable, self-associate,

270 reases the population of on- and off-pathway folding intermediates that could provide an important so

271 However, folding intermediates that exist at the native side of t

272 on of scattered hydrophobic residues in late folding intermediates that remain after early burial of

273 We propose that within folding intermediates the sign of the B8 phi angle exert

274 ions at positions known to stabilise the Im7 folding intermediate through non-native interactions.

275 y change for the dissociation of the dimeric folding intermediate to two monomeric intermediates is 1

276 tures, CYT-18 may also interact with earlier folding intermediates to avoid RNA misfolding or to trap

277 Second, there is a failure of CCT-generated folding intermediates to stably interact with TBCB, one

278 oproteins and reglucosylates them, returning folding intermediates to the cycle.

279 ting conformation has been linked to protein-folding intermediates, to biological function, and more

280 se contrast revealed that the misfolding and folding intermediates transiently self-organize into spa

281 tertiary interactions stabilize the compact folding intermediates under conditions in which the RNA

282 ty control within the ER by interacting with folding intermediates via their monoglucosylated glycans

283 L, they bound efficiently, indicating that a folding intermediate was significantly populated even wi

284 A cytochrome c kinetic folding intermediate was studied by hydrogen exchange (H

285 To search for folding intermediates, we have examined the folding and

286 No new folding intermediates were observed.

287 Conformational properties of the folding intermediates were probed by H/D exchange pulsed

288 Folding intermediates were trapped kinetically by acid q

289 zymes by promoting the formation of unstable folding intermediates, which is then followed by a casca

290 d codons are associated with cotranslational folding intermediates, which may be smaller than a singl

291 e suggests that highly dynamic, polydisperse folding intermediates, which occur during fibril formati

292 ulfide structure of a given cystinyl protein folding intermediate, while the HDX methodology can be u

293 ng helices that are formed in the on-pathway folding intermediate, whilst the smallest cluster forms

294 channel involves a stable, highly structured folding intermediate whose kinetic properties are better

295 ormed, sparsely populated compact on-pathway folding intermediate whose structure was elucidated prev

296 t a single-molecule level along with triplex folding intermediates, whose characterization has been c

297 red, form the same distinct helix plus sheet folding intermediate with the same time constant.

298 PTI) is characterized by the predominance of folding intermediates with native-like structures.

299 lvation occur prior to the population of the folding intermediate, with key regions involved in docki

300 te that Mss116 stabilizes an early, obligate folding intermediate within intron domain 1, thereby lay