ライフサイエンスコーパス: globular protein

1 target by associating more rapidly than the globular protein.

2 ctural domain; i.e., IRF-3 is a three-domain globular protein.

3 BD was rapid compared with that of a typical globular protein.

4 ata is close to that expected for an ~42 kDa globular protein.

5 uilibrium thermodynamic stability of a small globular protein.

6 ng effects on the equilibrium stability of a globular protein.

7 ate internal long-range contacts in this non-globular protein.

8 ial events underlying amyloid formation by a globular protein.

9 we extend the consensus strategy to design a globular protein.

10 s NMR spectra are characteristic of a folded globular protein.

11 traditional hydrophobic core expected for a globular protein.

12 s expected for a normal cooperatively folded globular protein.

13 like short oligonucleotide and a sphere-like globular protein.

14 tworks following thermal denaturation of the globular protein.

15 of the folding pathways of a large number of globular proteins.

16 tes, unlike results from previous studies on globular proteins.

17 of IDPs is generally no slower than that of globular proteins.

18 appears to be stronger in GFP than in other globular proteins.

19 account for pH effects on the properties of globular proteins.

20 ehavior with a complexity similar to that of globular proteins.

21 -helical intermediates in the folding of all globular proteins.

22 vent molecular dynamic simulations for three globular proteins.

23 sets these aggregates apart from most native globular proteins.

24 beta(32-42) fibrils is a common structure in globular proteins.

25 ent alone is insufficient for detecting most globular proteins.

26 ork for describing the folding mechanisms of globular proteins.

27 determine the size of the excess cavities in globular proteins.

28 mmonly found for the mechanical unfolding of globular proteins.

29 iophysical properties distinct from those of globular proteins.

30 zable groups are quite rare in water-soluble globular proteins.

31 pected to promote the cooperative folding of globular proteins.

32 formational substates of the native basin of globular proteins.

33 relate this phenomenon to cold unfolding of globular proteins.

34 ostatic pressure, similar to the behavior of globular proteins.

35 rials generated from synthetic polymers than globular proteins.

36 e boundaries for solutions of coarse-grained globular proteins.

37 ribution functions of water molecules around globular proteins.

38 imilar to free energies of folding for small globular proteins.

39 understand the folding process of many small globular proteins.

40 the stability, solubility, and solvation of globular proteins.

41 ghly ordered, similar to those of helices on globular proteins.

42 havior will be observed in many, if not all, globular proteins.

43 ccuracies comparable to sequence recovery in globular proteins.

44 s for the variation in compressibility among globular proteins.

45 tive state typical of those found for normal globular proteins.

46 polymers of the prion domain fused to other globular proteins.

47 ecular dynamics but also for a larger set of globular proteins.

48 residue values determined from databases of globular proteins.

49 omogeneous nucleation typically observed for globular proteins.

50 packed tertiary structure of natively folded globular proteins.

51 forces that are the highest yet reported for globular proteins.

52 e tested the approach on a diverse set of 28 globular proteins.

53 itting sensing and characterization of small globular proteins.

54 olar attractions are more important than for globular proteins.

55 former two types of filaments assemble from globular proteins.

56 ciples of in vivo amyloid fibrillogenesis by globular proteins, a previously obscure process.

57 r repetitive construction means that, unlike globular proteins, a repeat protein's equilibrium foldin

58 In contrast to globular proteins, a single protein sequence can aggrega

59 cifically to discriminate transmembrane from globular proteins, a very low overall false positive rat

60 from Sulfolobus solfataricus (Sso AcP) is a globular protein able to aggregate in vitro from a nativ

61 Tat system catalyzes the transport of folded globular proteins across the bacterial plasma membrane a

62 that have properties distinct from standard globular protein aggregators.

63 the Protein Data Bank contains some 100,000 globular protein and 3,000 membrane protein structures,

64 complexity of the dynamic native state of a globular protein and directly probe the residual frustra

65 ena, we have used chimeras of a well studied globular protein and exon 1 of huntingtin.

66 ficant number of beta-turn residues in every globular protein and the frequent deviation of beta-turn

67 etween the overall structural integrity of a globular protein and the local destabilization of its am

68 ormation for all types of local structure in globular proteins and a web server for local structure p

69 lready been used to characterize fibrils and globular proteins and are being increasingly used to stu

70 Allostery is an intrinsic property of many globular proteins and enzymes that is indispensable for

71 il reaching 20% at 10h with disappearance of globular proteins and generation of low molecular weight

72 ed the average residue compositions of OMPs, globular proteins and IMPs separately using a training s

73 endencies to appear in interior positions in globular proteins and in deeply buried positions of memb

74 ...pi interactions are often observed within globular proteins and in protein complexes, and examinat

75 rane proteins (OMPs) from non-OMPs (that is, globular proteins and inner membrane proteins (IMPs)).

76 bic core drives the folding of water-soluble globular proteins and is a key determinant of protein st

77 s that solution-phase conformations of small globular proteins and large molecular protein assemblies

78 crystallization of larger particles, such as globular proteins and nanoparticles, where interparticle

79 ermediary compactness of the protein between globular proteins and random coil polymers.

80 etween the Mr and EM diameter for a range of globular proteins and the intact virions.

81 coupled interactions can form in the DSE of globular proteins, and can involve residues that are dis

82 homology modelling software is optimized for globular proteins, and ignores the constraints that the

83 selective biomembrane channels/transporters, globular proteins, and ionophoric compounds, as well as

84 gest that this activity is intrinsic to many globular proteins, and that it must be enhanced to demon

85 Cold denaturation is a general phenomenon in globular proteins, and the associated cold-denatured sta

86 ic interactions are known to be important in globular proteins, and the possibility that they might p

87 Cold denaturation is a general property of globular proteins, and the process provides insight into

88 domains are conspicuous structural units in globular proteins, and their identification has been a t

89 rate and transition-state analysis of small globular proteins; and DOGMA, a web-server that allows c

90 hitectures showed that structural classes of globular proteins appeared early in evolution and in def

91 It has been demonstrated that like most globular proteins, AR proteins exhibit a two-state, coop

92 y structure is essential to the formation of globular protein architecture.

93 ostulates that structures and stabilities of globular proteins are determined by their amino acid seq

94 n be determined from x-ray diffraction, many globular proteins are not as easily structured.

95 Globular proteins are not permanently folded but spontan

96 It is now recognized that unfolded states of globular proteins are not random coils but instead can c

97 Residue fluctuations in globular proteins are shown to be more accurately predic

98 rates of confusion with signal peptides and globular proteins are the lowest among the tested method

99 ave unique elongated structures that, unlike globular proteins, are quite modular.

100 ded proteins into vesicles that incorporates globular proteins as building blocks.

101 a wide range of food products with gluten or globular proteins as functional agents.

102 ul in rationalizing the folding behaviour of globular proteins, as this representation provides intui

103 e average solvent exposure of amino acids in globular proteins, as well as with polarity indices and

104 entropy determines the thermal stability of globular proteins at ambient pressure.

105 excluded by these macromolecules stabilizes globular proteins because the native state occupies less

106 The functional native states of globular proteins become unstable at low temperatures, r

107 in-water (O/W) nanoemulsions stabilised by a globular protein (beta-lactoglobulin) for encapsulating

108 n-water nanoemulsions stabilized by either a globular protein (beta-lactoglobulin) or a non-ionic sur

109 e presence of high concentrations of a small globular protein, bovine pancreatic trypsin inhibitor (B

110 Finally, we also encapsulate a model globular protein, bovine serum albumin, and calculate it

111 Cold denaturation is a general property of globular proteins, but it is difficult to directly chara

112 We have devised several mechanical models of globular proteins by approximating them to various polyh

113 tudy the effects of pH on the charge of four globular proteins by expanding their surface charge dist

114 st to the commonly observed stabilization of globular proteins by ligand binding.

115 The dynamics of globular proteins can be described in terms of transitio

116 Folding of globular proteins can be envisioned as the contraction o

117 It was demonstrated that globular proteins can be reliably identified using this

118 Ubiquitin, the other globular protein characterized using psi-analysis, also

119 he equilibrium constant for folding, for the globular protein chymotrypsin inhibitor 2 (CI2) in conce

120 s then used to quantify the stability of the globular protein chymotrypsin inhibitor 2 (CI2) in these

121 ed protein, alpha-synuclein (alphaSN), and a globular protein, chymotrypsin inhibitor 2 (CI2) were ex

122 be molecular dynamics simulations of a small globular protein, chymotrypsin inhibitor 2, in 8 M urea

123 eptides, because the formation of functional globular proteins comes at the expense of an inherent ag

124 ion of the structures that formed revealed a globular protein complex that localized to the DNA end c

125 HisH-hisF is a multidomain globular protein complex; hisH is a class I glutamine am

126 ne and Pro contents were low suggesting high globular protein concentrations.

127 ediate intramolecular interactions to confer globular protein conformation.

128 It utilizes a model of a globular protein connected, through a single point (smal

129 unfolding pathways of representatives of all globular protein consensus folds (metafolds).

130 Globular proteins contain cavities/voids that play speci

131 al product of a single-chain precursor, is a globular protein containing two chains, A (21 residues)

132 gy should be generally applicable to soluble globular proteins containing buried free-cysteine residu

133 Resonances from small (approximately 10 kDa) globular proteins containing the amino acid analogue 3-f

134 The hybrid constructs, which consist of a globular protein core surrounded by a monolayer of elect

135 planar in overall shape as opposed to their globular protein counterparts.

136 k, we examine the interaction of the simple, globular protein cytochrome C (Cyt C) with MPMN surfaces

137 rate unfolded chain conformations of a small globular protein, cytochrome c, in the presence of guani

138 ble tether that restricts the diffusion of a globular protein domain for the purpose of catalysis or

139 PA receptors within a deep cleft between two globular protein domains (domains 1 and 2).

140 explanation for the energetics of export of globular protein domains across membranes in the absence

141 g folds could encompass the full set used by globular protein domains.

142 co-protein effects in mixtures of gluten and globular proteins during heating at 100 degrees C.

143 Comparison with other globular proteins (e.g., lysozyme) reveals that on the t

144 The models have a number of similarities to globular proteins: each chain folds into a unique, but d

145 ple V --> A mutations were made in the small globular protein eglin c.

146 ystem for understanding the encapsulation of globular proteins, enzymes, or antibodies for potential

147 ermediates formed during the folding of many globular proteins, even though it lacks a typical hydrop

148 Most globular proteins exhibit a characteristic sigmoidal wat

149 Numerous methods for docking globular proteins exist, however few have been developed

150 8 is a small, dimeric, very highly conserved globular protein first identified as an integral part of

151 Globular proteins fold by minimizing the nonpolar surfac

152 e to determine the protein type (membrane or globular), protein fold recognition, generation of atomi

153 -ligand binding affinities, mutation induced globular protein folding free energy changes, and mutati

154 ted in the literature shows that well-packed globular proteins follow a scaling relation between the

155 duced folding can compete effectively with a globular protein for a common target by associating more

156 We conclude that NIS competes with globular proteins for association with SDS, making it po

157 olymorph are similar to what is observed for globular proteins for the core residues, whereas M35 exh

158 the unfolding kinetics of UMP/CMP kinase, a globular protein from Dictyostelium discoideum, serve as

159 Globular protein fusion at the C-terminus likewise enabl

160 vestigate the mechanical response of a small globular protein GB1.

161 element of parallel beta-sheet in the small, globular protein Gbeta1.

162 ortable to heterologous proteins such as the globular protein GFP (green fluorescent protein) via a p

163 Although the interfacial behavior of globular proteins has been extensively studied, experime

164 llisecond folding reactions observed in many globular proteins have been ascribed either to the forma

165 eferences between interacting helices within globular proteins have been studied extensively over the

166 Small globular proteins have many contacts between residues th

167 ractions between pre-formed coiled coils and globular proteins have not been systematically analyzed.

168 Globular proteins, however, fold and function in aqueous

169 tic refolding of a set of mutants of a small globular protein, HPr, in which each of the four phenyla

170 s that accompany partial denaturation of the globular protein, human alpha-lactalbumin.

171 he effects of macromolecular crowding by two globular proteins, i.e., bovine pancreatic trypsin inhib

172 of three biologically relevant systems: (i) globular proteins, (ii) lipid bilayers, and (iii) membra

173 Beta-2 microglobulin (beta2m) is a small globular protein implicated in amyloid fiber formation i

174 e determined for purified vicilin, the major globular protein in kidney beans using intrinsic fluores

175 KRAB domain does not exist as a well-folded globular protein in solution but may fold into an ordere

176 psids (which are structurally different from globular proteins in both shape and arrangement of multi

177 seful for quantifying the stability of other globular proteins in cells to gain a more complete under

178 uctured proteins (IUPs) to induce folding of globular proteins in cellular environments, we show that

179 the thermodynamic stability of single-domain globular proteins in concentrated aqueous solutions.

180 e specific hydration sites on the surface of globular proteins in terms of the local water density at

181 as intrinsically disordered proteins (IDPs), globular proteins in the unfolded basin and during foldi

182 s is caused by misfolding and aggregation of globular proteins in vivo for which effective treatments

183 would be required to denature typical small, globular proteins in water.

184 of KIX has all the structural features of a globular protein, including three alpha-helices, two sho

185 as observed experimentally in association of globular proteins (insulin and a monoclonal anti-insulin

186 Myoglobin is a globular protein involved in oxygen storage and transpor

187 In this study, we show that a typical globular protein is able to undergo significant changes

188 tal results suggests that the folding of non-globular proteins is accurately described by a funneled

189 rates that structure prediction accuracy for globular proteins is limited mainly by the ability to sa

190 The unfolded state of globular proteins is not well described by a simple stat

191 a decrease expected from typical models for globular proteins, is a clear demonstration of parallel

192 es the construction of a CG model of a small globular protein, its simulation via Langevin dynamics,

193 water is important for the self-assembly of globular proteins, lipid membranes, nucleic acids, and o

194 es for hydration sites on the surface of two globular proteins, lysozyme and staphylococcal nuclease.

195 proteinase-1 cleavage sites, and full-length globular proteins [mCherry and leukemia inhibitory facto

196 s to simulate a representative sample of all globular protein metafolds under both native and unfoldi

197 a portion of mutational robustness in small globular proteins might have arisen by a process of neut

198 of amino-CLIO and ferritin), the weights of globular proteins (molecular weight of IgG and albumin),

199 of complete secondary-structure elements in globular proteins-molecular events that have previously

200 of a His tag to the N-terminus of the robust globular protein myoglobin leads to only minor changes t

201 orithm runs in O(n(10)/epsilon(6)) time, for globular protein of length n, and it detects alignments

202 o those of lysozyme that is taken as a model globular protein of similar molecular mass.

203 guishable (based on m-values) from that of a globular protein of similar size.

204 lecular mass higher than that expected for a globular protein of similar size.

205 ic volumes significantly larger than typical globular proteins of similar mass, thus imparting a bulk

206 dynamic stabilities only slightly lower than globular proteins of similar size.

207 The Amide I contours of six globular proteins of varied secondary structure content

208 ble range of folding rates for single-domain globular proteins of various size and stability, and tha

209 ssibility of the hydration shell surrounding globular proteins on differential contributions from cha

210 We quantified the effect of crowding by globular proteins on the equilibrium thermodynamic stabi

211 y bimodal while those obtained by trapping a globular protein or individual fluorophores are not.

212 Friction within globular proteins or between adhering macromolecules cru

213 ipper coiled coils were combined with either globular proteins or elastin-like polypeptides as recomb

214 or-rates for confusing membrane helices with globular proteins or signal peptides.

215 ue to fibrillation of disulfide-cross-linked globular proteins otherwise unrelated in sequence or str

216 -helical intermediates during the folding of globular proteins predicts previously unrecognized featu

217 studies mining these domain dictionaries for globular protein properties.

218 roteins, these proteins do not contain known globular protein-protein binding domains.

219 ates of spontaneous folding of single-domain globular proteins range from microseconds to hours: the

220 ates that the early stages of folding of all globular proteins, regardless of their native structure,

221 -helical intermediates in the folding of all globular proteins, regardless of their native structure.

222 In contrast to globular proteins, repeat proteins are stabilized only b

223 Although degradation of globular proteins requires ATP hydrolysis, the PAN-20S c

224 Application to the amide I region of a small globular protein reveals regions associated with the alp

225 irst native-like pore-forming protein, small globular protein (SGP).

226 These facts suggest that globular proteins should be maximally stable around room

227 Recent studies of globular protein solutions have uniformly adopted a coll

228 ize, in contrast to that observed in typical globular protein solutions, is observed to remain nearly

229 es the apparent viscosity of surfactant-free globular protein solutions, it is demonstrated here that

230 ded volume effect, similar to that found for globular protein solvents.

231 other existing methods in the predictions of globular protein stability changes upon mutation.

232 A resolution revealed a mainly alpha-helical globular protein stabilized by four antiparallel beta-sh

233 The structure of Der p 23 is a small, globular protein stabilized by two disulphide bonds, whi

234 rt the structure of a GNAT in complex with a globular protein substrate solved to 1.9 A.

235 exhibit properties expected of native like, globular proteins such as a single oligomerization state

236 gnitude and the translocation speed of small globular proteins such as ubiquitin by more than two ord

237 to the major secondary structure elements of globular proteins such as ubiquitin, whose resistance to

238 Globular proteins, such as cytochrome c (cyt c), display

239 We have demonstrated that globular proteins, such as hen egg lysozyme in phosphate

240 so designed to encapsulate and release bulky globular proteins, such as mCherry, in a light-dependent

241 rk model has been found to be valid for many globular protein systems.

242 etween anionic polyelectrolytes and cationic globular proteins takes place, such as the pathological

243 ticular, ribonuclease HI (RNase H), an 18 kD globular protein that hydrolyzes the RNA strand of RNA:D

244 The FT gene encodes a small globular protein that is able to translocate from the le

245 a small, dimeric, and very highly conserved globular protein that is an integral part of the dynein

246 Actin is ubiquitous globular protein that polymerizes into filaments and for

247 ne and human serum albumin (BSA and HSA) are globular proteins that function as bloodstream carriers

248 able objects (e.g., nanoparticles, micelles, globular proteins) that can adapt their shape to the loc

249 A point mutation of a small globular protein, the C-terminal domain of L9 destabiliz

250 In contrast to the case for globular proteins, the conformations of parallel and ant

251 biophysical phenomena such as the folding of globular proteins, the opening and closing of ligand-gat

252 It is also observed that for almost all globular proteins, the quality of contact prediction dic

253 In contrast to globular proteins, the structure of repeat proteins is d

254 ents were constructed with data derived from globular proteins, they perform poorly when applied to T

255 n of H-bonded beta-sheet, is achieved, as in globular proteins, through a balance of stabilizing and

256 whether a high shear can destabilize a small globular protein to any measurable extent.

257 iposome surfaces and find the DW dynamics on globular proteins to be significantly more heterogeneous

258 tion as a monomer, and the ability of molten globular proteins to carry out complex reactions.

259 rotein design to create an extremely stable, globular protein, Top7, with a sequence and fold not obs

260 surface (FES) of the native basin of a small globular protein, Trp-cage.

261 Globular proteins typically fold into tightly packed arr

262 kinase PINK1 phosphorylates the well-folded, globular protein ubiquitin (Ub) at a relatively protecte

263 The small globular protein, ubiquitin, contains a pair of opposite

264 different force-field configurations for two globular proteins, ubiquitin and the gb3 domain of prote

265 this being the first solution structure of a globular protein under pressure.

266 f amyloid aggregate formations by structured globular proteins under conditions close to physiologica

267 dodecyl sulfate (SDS) denatures and unfolds globular proteins under most conditions.

268 an charge states and charge distributions of globular proteins under non-denaturing and denaturing co

269 e rapidly and more effectively than standard globular proteins under similar conditions.

270 Here, we investigate whether globular proteins unfolded by SDS can be refolded upon a

271 In contrast, globular proteins unfolded under less denaturing conditi

272 The globular protein unfolds reversibly with a T(m) of 102.8

273 suggested nucleation of folding of cytosolic globular proteins vectorially from hydrophilic N to hydr

274 on, QSOX is unable to cross-link well-folded globular proteins via their surface thiols.

275 the distribution of local fluctuations in a globular protein was monitored in response to localized,

276 macromolecular crowding on the behavior of a globular protein, we performed a combined experimental a

277 To extend this result to a more globular protein, we present an investigation of the dim

278 Because of these similarities to globular proteins, we believe that the polyhedral models

279 om a study of 119 all-beta folds observed in globular proteins, we have now determined that, if PrP(S

280 ng from nature's amazing molecular machines, globular proteins, we present a framework for the predic

281 dynamics trajectory of a small fast folding globular protein; we briefly describe the thermodynamic

282 The fast dynamics of the four globular proteins were found to be sensitive to solution

283 s and the surface hydrophobicity of unfolded globular proteins were the main characteristics in deter

284 The intrinsic protein characteristics of globular proteins which enhance polymerization in mixtur

285 Thus, for globular proteins, which have much higher variation in l

286 fatal disease caused by misfolding of native globular proteins, which then aggregate extracellularly

287 ophobic collapse for an unstructured and two globular proteins while directly measuring initial cotra

288 the Abeta(1-40) fibril core is atypical for globular proteins, while in contrast, the antiparallel b

289 our studies define an "Achilles' heel" in a globular protein whose repair may enhance the stability

290 idering bovine serum albumin because it is a globular protein whose solution properties have also bee

291 ke polyelectrolyte, and lysozyme, a cationic globular protein with a charge that can be genetically m

292 CooA is a globular protein with an Ig fold and is similar in struc

293 cells using a variant of protein L, a 7 kDa globular protein with seven lysine residues replaced by

294 s and compare the measurements of a hydrated globular protein with the results of a coarse-grained mo

295 ed for crystallography; "C" indicates folded globular proteins with broadened line shapes; and "D" ar

296 rating the potential for consensus design of globular proteins with increased stability, these result

297 Beta-2 Microglobulin (beta2m) is a small, globular protein, with high solubility under conditions

298 Facile diffusion of globular proteins within a cytoplasm that is dense with

299 at this is a universal property of all small globular proteins without prosthetic groups.

300 Insulin provides a classical model of a globular protein, yet how the hormone changes conformati