ライフサイエンスコーパス: molten globule

1 ics ascribed to the recently postulated "dry molten globule".

2 Thus, it has some features of a molten globule.

3 low-pH urea unfolded state, but it is not a molten globule.

4 he properties of an intrinsically disordered molten globule.

5 n contrast, apoFixLH presented features of a molten globule.

6 to the alpha-helical nature of the alpha-LA molten globule.

7 red form, suggesting that it forms a helical molten globule.

8 phobic surfaces that are characteristic of a molten globule.

9 tes such as fully folded, fully unfolded, or molten globule.

10 s of structural heterogeneity in the kinetic molten globule.

11 ingle molecule with the characteristics of a molten globule.

12 antly destabilized compared to the wild-type molten globule.

13 actalbumin exhibits the characteristics of a molten globule.

14 fold of the alpha-domain is preserved in the molten globule.

15 ity of individual helices in stabilizing the molten globule.

16 es that are crucial for the stability of the molten globule.

17 olvent accessibility of other regions of the molten globule.

18 o folding that has long been thought to be a molten globule.

19 tive conformation reminiscent of the protein molten globule.

20 e entry domain exhibits characteristics of a molten globule.

21 of the alpha-domain to the stability of the molten globule.

22 rtially folded protein intermediates such as molten globules.

23 f interactions between the apical domain and molten globules.

24 luence the protein folding pathways from the molten globules.

25 e disulfide bridges and the establishment of molten globules.

26 ed to produce partially unfolded equilibrium molten globules.

27 ty of the core, suggesting that they are dry molten globules.

28 ocess results in the formation of aggregated molten globules.

29 ers maintaining properties of intermolecular molten globules.

30 The molten globule +8 shows a very specific transition.

31 The molten globule, a conformational ensemble with significa

32 han that found previously for the archetypal molten globule, alpha-lactalbumin (alpha-LA); this diffe

33 ggest a possible link between an equilibrium molten globule and a functional intermediate that may be

34 context of previous studies of the alpha-LA molten globule and can be used to reconcile apparent dis

35 l ordered, demonstrating that S-824 is not a molten globule and forms a unique structure.

36 e-chain proton jump motion is reduced in the molten globule and in the denatured proteins when compar

37 ceptor activation by light converts PYP to a molten globule and indicate stimulus-induced unfolding t

38 ce, the slowest step is unfolding of the wet molten globule and involves a solvated transition state.

39 mental data available for the human alpha-LA molten globule and its more denatured states.

40 ng to misfolding, the barrier separating the molten globule and native states increases, although the

41 he conformation changes that distinguish the molten globule and native states of apomyoglobins origin

42 biased simulations and used as models of the molten globule and partly denatured states of human alph

43 mer, dextran, lead to increased formation of molten globule and stabilizes the protein with respect t

44 Differences between the pH 4 equilibrium molten globule and the kinetic intermediate are evident:

45 alpha-LA remain significantly buried in the molten globule and the side-chain dynamics of these resi

46 suggest that these are general properties of molten globules and could have important implications fo

47 unt for the dramatic compaction observed for molten globules and the "physiological" unfolded state.

48 results suggest that the rapid formation of molten globules and the variable behavior of those globu

49 kin to ANS, which fluoresces upon binding to molten globules and thermal denaturation intermediates.

50 erent states: native-like, partially folded (molten globule) and completely unfolded, following two d

51 phan residue were investigated under native, molten globule, and unfolded conditions.

52 guiding a large structural transition from a molten globule apo-state to a compact holoconformation.

53 Molten globules are partially folded forms of proteins t

54 artially folded intermediate states, such as molten globules, are compliant and can deform elasticall

55 after a rapid jump to native conditions) and molten globules (arising due to mutations or cosolvents)

56 nduced unfolding to a partially unstructured molten globule as a novel theme in signaling.

57 tion (G20R), by contrast, leads to a dimeric molten globule, as indicated by its 1H-NMR features and

58 tate is compact and has characteristics of a molten globule, as shown by its retention of significant

59 in the native state of the protein, not the molten globule, as shown by x-ray crystallography.

60 nd 15N chemical shifts of the human alpha-LA molten globule at 50 degrees C leads to the identificati

61 sical studies have shown that StAR becomes a molten globule at acidic pH, but a physiologic role for

62 um of the human alpha-lactalbumin (alpha-LA) molten globule at pH 2 and 20 degrees C is characterised

63 e the structural preferences of the alpha-LA molten globule at pH 7 at the level of individual residu

64 The molten globule at pH 7 is generally less stable than tha

65 ational ensemble that describes the alpha-LA molten globule at these two pH values.

66 isolate and characterize the observed stable molten globule, (b) to analyze the heterogeneity of fold

67 We propose that "local" molten globule behavior optimizes detoxication enzymes.

68 -bundle protein that forms collapsed, stable molten globules but lacks a uniquely folded structure-tr

69 Under native conditions, free pVHL is a molten globule, but it is stabilized in the E3 complex.

70 The molten globule characteristics of NCBD are thus restrict

71 Herein, we further characterize the molten globule characteristics of T. maritima IscU by ne

72 The molten globule characteristics of the C-terminal domain

73 that the almost fully folded protein retains molten globule characteristics with severe NMR line broa

74 artially structured Zn(2+)-bound domain with molten globule characteristics, and a stable, well-order

75 ha-helix-rich monomeric precursor state with molten globule characteristics, converting in vitro into

76 pecies result in an inactive apoprotein with molten-globule characteristics.

77 onclude that at pH 4-5, 3betaHSD2 takes on a molten globule conformation that promotes the dual funct

78 n alpha-lactalbumin (alpha-LA) that adopts a molten globule conformation under near physiological con

79 illebrand disease mutations induce misfolded molten globule conformations of the A1 domain.

80 of the A1 domain to misfold to pathological molten globule conformations that differentially alter t

81 transient hydrophobic interactions with the molten globule core.

82 ues that may influence the properties of the molten globule differently at low and neutral pH.

83 he light chain acquires a novel pre-imminent molten-globule enzyme conformation at the physiologicall

84 The pre-imminent molten-globule enzyme form also exhibited the maximum en

85 a well-defined structure and behaves like a molten globule, even in the presence of Zn(2+), and that

86 although at pH 4 the native protein forms a molten globule folding intermediate in which the histidi

87 assumption that many other proteins populate molten globule folding intermediates.

88 elucidate structure in both the burst-phase molten globule-folding intermediate of apomyoglobin and

89 on ligation, similar to a previously studied molten globule form induced by low pH.

90 s has been shown to convert the protein into molten globule form(s), which can undergo both heat-indu

91 1)-AT involves a cooperative transition to a molten globule form, followed by a non-cooperative trans

92 K mutation stabilizes an intermediate of the molten-globule form of the repressor, increasing exposur

93 ein that results in a compact structure) and molten globule formation (the formation of stable, react

94 Thus, molten globule formation in human alpha-lactalbumin can

95 NA folding and the "burst phase" changes and molten globule formation in protein folding.

96 contents that are comparable to that of the molten globule formed by porphyrin cytochrome c under si

97 f apoleghemoglobin at least, the equilibrium molten globule formed under destabilizing conditions at

98 ce of the equilibrium between the native and molten globule forms.

99 The apomyoglobin molten globule has a complex, partly folded structure wi

100 ly disordered kinetic trap, interpreted as a molten globule, has a wide temperature range of metastab

101 ating that longer-range perturbations of the molten globule have occurred.

102 Since molten globules have been implicated in both normal and

103 re becomes solvated only later in a late wet molten globule, IL, which precedes the unfolded form.

104 ically structured energy landscape to form a molten globule in a few seconds.

105 a model for the alpha-lactalbumin (alpha-LA) molten globule in a number of studies.

106 and, to a lesser degree, in formation of the molten globule in guanidine hydrochloride, but not in th

107 d Escherichia coli enzyme, which exists as a molten globule in the absence of ligands, and a well fol

108 teractions are required to generate a stable molten globule in the two lysozymes.

109 sistent with the bipartite structure for the molten globule in which the A, G, and H helices are stab

110 We propose a model of the apoE4 molten globule in which the four-helix bundle of the ami

111 sulfide mutants are less stable and exist as molten globules in the monomeric state.

112 Despite the importance of molten globules in understanding the mechanisms of prote

113 cin Ia channel domain may be described as a "molten globule", in which the helical secondary structur

114 mes accentuates the conversion of apoE4 to a molten globule, inducing reactive intermediates capable

115 sion to VWF in hemostasis, unfolds through a molten globule intermediate in an apparent three-state m

116 se results suggest that the structure of the molten globule intermediate of apoleghemoglobin is more

117 t support to the hypothesis that the kinetic molten globule intermediate of apoMb is native-like.

118 L/ES and protease Lon compete for binding to molten globule intermediate of DHFR, resulting in a pecu

119 tes the formation of a compact and transient molten globule intermediate state.

120 ter than that observed for the highly pliant molten globule intermediate states.

121 s the unfolding mechanism by eliminating the molten globule intermediate that is seen in wild type un

122 rs exhibits many of the characteristics of a molten globule intermediate with some helical character

123 g transition state to the value found in the molten globule intermediate.

124 The kinetic and equilibrium molten globule intermediates formed by N132G/E136G are s

125 ly in folding of this RNA is grossly akin to molten globule intermediates in protein folding.

126 dies, and the average histidine pK(a) in the molten globule is determined from the pH dependence of t

127 unfolded protein indicates that the alpha-LA molten globule is highly heterogeneous; each residue has

128 formation on the structure and dynamics of a molten globule is limited, largely because of the high c

129 olvent accessibility of W118 in the alpha-LA molten globule is lower than that in the native state.

130 state); this large compliance means that the molten globule is more deformable and the unfolding rate

131 lpha-lactalbumin (alpha-LA), the equilibrium molten globule is most often studied at pH 2, the so-cal

132 traordinary stability of the canine lysozyme molten globule is not due to an unusually stable isolate

133 on on enzymatically active molten-globule or molten-globule like structures.

134 hione transferase A1-1 (GSTA1-1), exploits a molten globule-like active site to achieve remarkable ca

135 ons with amphipathic helices form a dynamic, molten globule-like binding site and provide clusterin t

136 es 1 and 2 (MBI and MBII, respectively) have molten globule-like characteristics.

137 ls at low pH, where it adopted the classical molten globule-like conformation.

138 lowed by progressive unfolding of a compact, molten globule-like denatured state ensemble as the temp

139 weakly structured regions, such as loops and molten globule-like domains that are inaccessible in con

140 l N-terminal two-thirds of the apoprotein is molten globule-like in solution.

141 tudied helix formation in the binding of the molten globule-like nuclear coactivator binding domain a

142 -to-the-barrel ILV cluster (cluster 3) imply molten globule-like packing.

143 suggest that the redesigned protein exhibits molten globule-like properties, possibly because the red

144 domain, despite its reported aggregation and molten globule-like properties.

145 Induction of a low-pH-induced, molten globule-like state inhibited glycolipid intermemb

146 globule state, a result suggesting that the molten globule-like state is stabilized relative to the

147 the photoactivated form of OCP represents a molten globule-like state that is characterized by incre

148 autoinhibited homodimeric chaperones adopt a molten globule-like state that transiently exposes the s

149 ures up to 200MPa resulted in a structurally molten globule-like state where PepX maintained its seco

150 In its molten globule-like state, the domain resists degradatio

151 0, generating a conformationally fluctuating molten globule-like state.

152 s fully synthesized, without collapsing into molten globule-like states or forming stable intermediat

153 baseline region in the absence of populated molten globule-like states.

154 NMR studies suggest a molten globule-like structure also in the dimeric state.

155 -4 and C(H)2 domains, which unfold to form a molten globule-like structure that is aggregation-prone.

156 Thus, NaClO(4) denatures by inducing a molten globule-like structure that seems completely off-

157 of Mg(2+) and Ca(2+), CaBP1 forms a flexible molten globule-like structure.

158 etal-free DREAM adopts a folded yet flexible molten globule-like structure.

159 size exclusion chromatography suggest a pre-molten globule-like structure.

160 rmation of arrestin-1, possibly to a dynamic molten globule-like structure.

161 three long regions of natively disordered or molten globule-like structures containing putative amphi

162 large tetrameric enzyme DAHP synthase to a 'molten globule-like' region surrounding the active site.

163 ediate was attributed to the appearance of a molten-globule-like (MG) state.

164 NS), we show that RBP populates a state with molten-globule-like characteristics early in refolding.

165 In order to understand the origins of this molten-globule-like compaction, we have characterized a

166 folding traps these proteases into inactive molten-globule-like conformers that switch into active e

167 d, and the C terminus appears to behave as a molten-globule-like structure whose folding is tightly c

168 ial abilities of the apoE isoforms to form a molten globule may contribute to the isoform-specific ef

169 rarr2;MG) leading to a transiently populated molten globule (MG) state.

170 f the folding transitions from native (N) to molten globule (MG) to kinetic intermediates (U) pathway

171 rmediates, of which an important type is the molten globule (MG).

172 adopted by these intermediates, also called molten globules (MG), to understand protein folding.

173 te may not be the best model for the kinetic molten globule observed during refolding of alpha-LA.

174 e-chain dynamics of aromatic residues in the molten globule of alpha-LA.

175 fferences from the well-characterized pH 4.1 molten globule of apoMb.

176 The hydrogen-exchange behavior of the low-pH molten globule of human alpha-lactalbumin, containing al

177 etailed characterization of the acid-induced molten globule of RBP is presented.

178 insight into the structural features of the molten globule of RBP, we have monitored the denaturant-

179 Substitutions G20R and G20A lead to dimeric molten globules of low stability, suggesting that the im

180 ce in comparisons of equilibrium and kinetic molten globules of other proteins.

181 s, we show that the dense phase has either a molten globule or a crystalline structure, depending on

182 nd may be viewed as consistent with either a molten globule or fully folded state.

183 h the idea that empty MHC molecules exist as molten globules or other partially unfolded intermediate

184 vide new information on enzymatically active molten-globule or molten-globule like structures.

185 Betanova's structure appears to be molten globule over the 3-82 degrees C temperature range

186 y, the unfolded state, the native state, the molten globule phase (MG), and the surface interaction-s

187 nd proton exchange that was characterized in molten globule predecessors.

188 protein did not exhibit any non-native-like molten globule properties despite the large number of mu

189 Structural investigations of molten globules provide an important contribution toward

190 accomplished primarily by destabilizing the molten globule rather than stabilizing the metastable na

191 oinhibition where the activation box and the molten globule region act synergistically to impair the

192 The molten globule region and the activation box become less

193 onal autoinhibitory element in the form of a molten globule region within the linker between RGSL and

194 distributions for pressure- and pH-populated molten globules shows them to be remarkably similar desp

195 ion of the structure, generating a monomeric molten globule species that retains its native helical c

196 Molten globule stability is measured by reversible urea

197 nce with the G23A/G25A double mutant affects molten globule stability to an intermediate extent, conf

198 of the A and G helices both strongly affect molten globule stability, in contrast to results for the

199 gative in sign over the temperature range of molten globule stability.

200 sed NMR studies reveal that OBP4 exists in a molten globule state and binding of indole induces a dra

201 n studied to elucidate the energetics of the molten globule state and its contribution to the stabili

202 The dynamics of the acid unfolded and molten globule state are similar in the framework of the

203 , and toxins such as colicin A unfold to the molten globule state at bacterial surfaces before insert

204 In the molten globule state at pH 2, tauR is 2.5 microsec, incr

205 l flexibility and exists in a highly dynamic molten globule state at physiological temperature.

206 3)) is characteristic of a partially folded, molten globule state expected to contain partial seconda

207 he structure and dynamics of the equilibrium molten globule state formed at pH 4.1 have been examined

208 g between the initial unfolded state and the molten globule state formed either kinetically during re

209 ization of the overall fold showing that the molten globule state has a degree of global cooperativit

210 folding and stability, although a link to a molten globule state has not previously been shown.

211 es to capture the formation of the ephemeral molten globule state in protein L, which has never been

212 helices of alpha LA are capable of forming a molten globule state in the absence of the remainder of

213 B, D, and 3(10) helices are known to form a molten globule state in the absence of the rest of the p

214 The molten globule state is a partially folded conformer of

215 s in the pressure range of 0-3 kbar, where a molten globule state is formed.

216 nfolded and presence of alpha-helices in the molten globule state lead to internal friction to a simi

217 modynamically unstable and several acquire a molten globule state near human physiological temperatur

218 zation by direct binding to concavity in the molten globule state of a protein.

219 ogether, these findings demonstrate that the molten globule state of alpha-LA is an ensemble of confo

220 onsistent with an experimental report of the molten globule state of ApoE4, simulations identify mult

221 Unlike natively folded proteins, the molten globule state of apomyoglobin is compliant (large

222 rmation on the urea-induced unfolding of the molten globule state of bovine alpha-lactalbumin (BLA) h

223 ble of subcompact conformers, similar to the molten globule state of human alpha-lactalbumin, demonst

224 The molten globule state of human serum retinol-binding prot

225 characteristics similar to those of the pH 2 molten globule state of the protein.

226 denatured state at pH 2.6 through the stable molten globule state pH approximately 4.1 to the folded

227 effect associated with the unfolding of the molten globule state reveal that it is negative in sign

228 d the alpha-domain is more structured in the molten globule state than is the beta-domain.

229 omain is considerably more structured in the molten globule state than the beta-subdomain.

230 transitions observed in PimA might reflect a molten globule state that confers to PimA, a higher affi

231 R binds to membranes in a partially unfolded molten globule state that is relevant to the activity of

232 into the membrane, which is favoured by the molten globule state under investigated acidic condition

233 ormation, which shows characteristics of the molten globule state under near physiological conditions

234 acteristic of the more compact, salt-induced molten globule state, a result suggesting that the molte

235 rd pH 2, at which alpha-lactalbumin adopts a molten globule state, a small but increasing proportion

236 At pH 3, the ovotransferrin adopted a molten globule state, associated with a significant incr

237 alpha-lactalbumin, which have features of a molten globule state, have been studied to elucidate the

238 R600M mutant has properties reminiscent of a molten globule state, including a tendency to aggregate,

239 itude of the signal of W104 decreases in the molten globule state, perhaps due to the protonation of

240 In the molten globule state, the magnitude of the fluorescence

241 In the molten globule state, there is an increase in the extent

242 All alpha-lactalbumins form a well populated molten globule state, while most of the lysozymes do not

243 alpha LA) forms a well-populated equilibrium molten globule state, while the homologous protein hen l

244 ts associated with the transition across the molten globule state.

245 of ligand, in vitro LUSH exists in a partial molten globule state.

246 ow that this acid-denatured species is not a molten globule state.

247 stinct conformations, possibly existing in a molten globule state.

248 pin or cholesterol in the membrane fosters a molten globule state.

249 is order changes to W60 > W104 > W118 in the molten globule state.

250 a class of intermediates referred to as the molten globule state.

251 urs when chicken cystatin is in its reduced, molten-globule state, implying that the organization of

252 long-distance contacts, thus resembling the "molten globule" state.

253 st in a wide range of conformations or in a "molten globule" state.

254 These proteins form two of the most stable molten globule states among all the lysozymes.

255 A close similarity between equilibrium molten globule states and kinetic species observed durin

256 Model proteins can exist in native and molten globule states and participate in functional and

257 rtant question in protein folding is whether molten globule states formed under equilibrium condition

258 three tryptophan residues in the native and molten globule states have different degrees of motional

259 eased exchange protection in the equilibrium molten globule states near pH 4.

260 low the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of h

261 ated the response to force of the native and molten globule states of apomyoglobin along different pu

262 ontrast to the dynamic but otherwise similar molten globule states of proteins.

263 observed differences in the behaviour of the molten globule states of the two proteins.

264 ompared to earlier experimental estimates in molten globule states, and is consistent with more recen

265 myoglobin, for the unfolded and even for the molten globule states, models from polymer science are e

266 Finally, from native to molten globule states, the hydration water networks loos

267 e traits are the distinguishing hallmarks of molten globule states, which have been intensively studi

268 l protein of apomyoglobin in both native and molten globule states.

269 ixtures of folded and unfolded species or as molten globule states.

270 ecule can be observed in both the native and molten globule states.

271 ropy decays of tryptophans in the native and molten globule states.

272 ical unfolding pathways at low force akin to molten globule states.

273 hypothesis that such intermediates resemble molten globule states; i.e. with native-like backbone hy

274 for the establishment of new topologies and molten globule states; their effects, however, can be in

275 myloid fibril formation, and not with stable molten globules states or amorphously aggregating specie

276 Apart from the native state, native-like and molten-globule states have been identified; these states

277 on of bis-ANS to quantify the population of "molten globule" states.

278 a strong correlation in the existence of the molten globule structure and optimum endopeptidase activ

279 ritical for the stabilisation of the compact molten globule structure.

280 tained that more closely resembled that of a molten globule, suggesting that the structure of the pro

281 e of apoMb at pH 6 has been referred to as a molten globule, the data presented here reveal significa

282 This transition from the helical molten globule to beta-conformation has striking similar

283 His-24 is not a barrier to refolding of the molten globule to the native protein.

284 l that StAR activity requires a pH-dependent molten globule transition on the OMM.

285 al changes that have been characterized as a molten globule transition.

286 This type of structure is characterized as a molten globule type conformation, which was further conf

287 enzymatically inactive BoNT/A did not show a molten globule type of structure.

288 is shown to possess a novel combination of a molten globule-type C-terminal domain and an N-terminal

289 ther proteins that were observed to sample a molten globule under similar conditions.

290 ative-favoring conditions proceeds through a molten globule unfolded monomer state, with a nucleation

291 in different conformational states (native, molten globule, unfolded) of apomyoglobins.

292 nsemble of structures that contribute as the molten globule unfolds and shows, in accord with experim

293 [28-111] alpha-LA forms a molten globule very similar to that formed by the wild-t

294 A stable intermediate compatible with molten globule was shown to exist along the pathways of

295 tween pH 3.0 and pH 4.0, is reminiscent of a molten globule, wherein tertiary structure contacts are

296 o the structure and dynamics of the alpha-LA molten globule, which serves as a prototype for partiall

297 one of its stable conformational states is a molten-globule, which retains over 60% of its optimal en

298 ain forms a folded structure or behaves as a molten globule will have a significant bearing on the me

299 esidual secondary structures, free NCBD is a molten globule with a helical content similar to that in

300 collectively is dramatically reduced in the molten globules with the correlation length being 6.9 A