ライフサイエンスコーパス: globular protein

1 anionic (e.g., DNA, ribosomes, RNA, and most globular proteins).

2 tworks following thermal denaturation of the globular protein.

3 target by associating more rapidly than the globular protein.

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

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

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

7 uilibrium thermodynamic stability of a small globular protein.

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

9 ial events underlying amyloid formation by a globular protein.

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

11 traditional hydrophobic core expected for a globular protein.

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

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

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

15 former two types of filaments assemble from globular proteins.

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

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

18 trinsically different from those observed in globular proteins.

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

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

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

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

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

24 vent molecular dynamic simulations for three globular proteins.

25 ly leads to a globular shape, thus mimicking globular proteins.

26 sets these aggregates apart from most native globular proteins.

27 its role in the onset of global dynamics in globular proteins.

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

29 ent alone is insufficient for detecting most globular proteins.

30 ork for describing the folding mechanisms of globular proteins.

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

32 sensitive to pressure than folded states of globular proteins.

33 mmonly found for the mechanical unfolding of globular proteins.

34 iophysical properties distinct from those of globular proteins.

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

36 pected to promote the cooperative folding of globular proteins.

37 formational substates of the native basin of globular proteins.

38 inkers can contract to similar dimensions as globular proteins.

39 relate this phenomenon to cold unfolding of globular proteins.

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

41 rials generated from synthetic polymers than globular proteins.

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

43 ribution functions of water molecules around globular proteins.

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

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

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

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

48 by native contacts in determining folding of globular proteins.

49 understand the folding process of many small globular proteins.

50 omogeneous nucleation typically observed for globular proteins.

51 packed tertiary structure of natively folded globular proteins.

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

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

54 itting sensing and characterization of small globular proteins.

55 olar attractions are more important than for 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 How is a water-soluble globular protein able to spontaneously cross a cellular

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 function, we report that ComW is a predicted globular protein and that it interacts with DNA, indepen

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

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

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

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

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

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

93 Globular proteins are not permanently folded but spontan

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

110 s succeeded in generating a large variety of globular proteins, but the construction of protein scaff

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

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

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

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

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

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

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

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

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

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

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

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

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

124 thod to characterize subunit interactions in globular protein complexes.

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

126 ediate intramolecular interactions to confer globular protein conformation.

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

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

129 Globular proteins contain cavities/voids that play speci

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

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

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

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

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

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

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

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

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

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

140 Transient, regulated binding of globular protein domains to Short Linear Motifs (SLiMs)

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 In addition, globular proteins (EB1 and PRC1) diffuse more slowly tha

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 Biomolecular force fields optimized for globular proteins fail to properly reproduce properties

151 8 is a small, dimeric, very highly conserved globular protein first identified as an integral part of

152 Globular proteins fold by minimizing the nonpolar surfac

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

154 isordered proteins appear to follow rules of globular protein folding, such as the cooperative nature

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

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

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

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

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

160 Globular protein fusion at the C-terminus likewise enabl

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

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

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

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

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

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

167 Small globular proteins have many contacts between residues th

168 As these small, globular proteins have many interactors, it has been dif

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

170 Globular proteins, however, fold and function in aqueous

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

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

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

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

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

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

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

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

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

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

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

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

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

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

185 and experiments for a diverse set of soluble globular proteins indicates that the cluster model appli

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

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

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

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

190 Amyloid formation of folded, globular proteins is commonly initiated by partial or co

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

192 is the primary effect driving the folding of globular proteins is nearly universally accepted (includ

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

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

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

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

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

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

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

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

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

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

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

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

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

206 =+3) is virtually as compact and stable as a globular protein of the same number of amino-acids.

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

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

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

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

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

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

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

214 Friction within globular proteins or between adhering macromolecules cru

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

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

217 ome of the classic paradigms established for globular proteins, pointing to important similarities in

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

219 studies mining these domain dictionaries for globular protein properties.

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

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

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

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

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

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

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

227 ted that the sizes of the unfolded states of globular proteins should decrease as the denaturant conc

228 multivalent ions in a net negatively charged globular protein solution (BSA) can either cause simple

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

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

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

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

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

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

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

236 ons based on contact statistics among folded globular protein structures reproduce the overall experi

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

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

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

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

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

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

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

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

245 ein fibronectin circulates in the blood as a globular protein that dimerizes through disulfide bridge

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

262 Globular proteins typically fold into tightly packed arr

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

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

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

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

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

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

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

270 In contrast, globular proteins unfolded under less denaturing conditi

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

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

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

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

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

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

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

278 However, in several soluble-globular proteins, we identified a class of nonconserved

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

296 mpare and contrast the folding mechanisms of globular proteins with the emerging features of binding-

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