ライフサイエンスコーパス: folding intermediate

1 tly correlates with the stability of the RNH folding intermediate.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

17 an excellent model for an obligatory kinetic folding intermediate.

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

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

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

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

22 eneity and diverse rearrangement pathways of folding intermediates.

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

24 ansitions to its stable native structure via folding intermediates.

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

26 facilitates the identification of pseudoknot folding intermediates.

27 abeling method for determining structures of folding intermediates.

28 tions are good structural models for kinetic folding intermediates.

29 ion while avoiding destruction of productive folding intermediates.

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

31 serves as a stabilizing scaffold for protein-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 ins and identification of stable two-helical folding intermediates.

38 ficiency reveals two previously undetermined folding intermediates.

39 s with the appearance of prophase chromosome folding intermediates.

40 roach for visualizing RNA folding states and folding intermediates.

41 determining the high-resolution structure of folding intermediates.

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

43 ding of barnase that involves two detectable folding intermediates.

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

45 se partial folds provide models of oxidative folding intermediates.

46 ons is not conclusive proof of thermodynamic folding intermediates.

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

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

49 in order to trap and characterize different folding intermediates.

50 seful tools for the characterization of LamB folding intermediates.

51 resolve closely spaced, transiently occupied folding intermediates.

52 ructural and energetic properties of kinetic folding intermediates.

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

54 asing the concentration of aggregation-prone folding intermediates.

55 ing structured populations in conformational folding intermediates.

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

57 ble details on the structures of equilibrium folding intermediates.

58 associated such codons with cotranslational folding intermediates.

59 e hybridization facilitates the detection of folding intermediates.

60 in characterizing the dynamic properties of folding intermediates.

61 ctive structure relative to compact inactive folding intermediates.

62 many other proteins populate molten globule folding intermediates.

63 would favor aggregation of unstable protein folding intermediates.

64 imerization proceeded through multiple, slow-folding intermediates.

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

66 estrated by PQC through the interaction with folding intermediates.

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

68 binding and stabilizing met-alpha hemichrome folding intermediates.

69 te between unfolded and partially structured folding intermediates.

70 at allows direct analysis of cotranslational folding intermediates.

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

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

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

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

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

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

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

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

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

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

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

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

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

84 Equilibrium dynamics of different folding intermediates and denatured states is strongly c

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

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

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

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

89 ructural determination of HP-induced protein folding intermediates and irreversible oligomerization.

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

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

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

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

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

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

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

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

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

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

100 Protein folding intermediates and transition states are commonly

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

118 Two folding intermediates are observed, the second of which

119 Protein folding intermediates are often imperative for overall f

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

143 These findings demonstrate that nascent folding intermediates can play an important role in dise

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

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

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

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

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

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

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

151 transient topological properties of nascent folding intermediates drive sequential chaperone associa

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

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

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

155 Although most folding intermediates escape detection, their characteri

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

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

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

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

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

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

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

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

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

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

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

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

168 The folding intermediate further acted as a template that fa

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

170 Folding intermediates have been detected and characteriz

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

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

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

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

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

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

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

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

179 4 the native protein forms a molten globule folding intermediate in which the histidine residues are

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

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

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

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

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

185 Potential folding intermediates in the formation of the microflore

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

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

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

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

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

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

192 nsin-mediated loops are lost and a transient folding intermediate is formed that is devoid of most lo

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

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

195 isingly, we found that population of the RNH folding intermediate is required to generate sufficient

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

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

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

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

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

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

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

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

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

205 How folding intermediates observed in vitro for the majority

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

224 2.2 A from wild-type VEGF, identifies a true folding intermediate of VEGF.

225 A folding intermediate of WT-beta(2)m, known as the I(T)-s

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

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

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

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

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

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

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

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

234 g assay to show that RNase H forms a similar folding intermediate on and off the ribosome.

235 ous energy (for example, ATP)(9), we trapped folding intermediates on this machine.

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 on mechanism involving unfolded proteins and folding intermediates when their levels exceed the foldi

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

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

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

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

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

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

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

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

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

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