ライフサイエンスコーパス: denatured protein

1 ibit growth by causing toxic accumulation of denatured protein.

2 y probability distributions for dye-labeled, denatured protein.

3 is possible by the addition of salts to the denatured protein.

4 aggregates than with aggregates of thermally denatured protein.

5 resistant to tryptic hydrolysis than is the denatured protein.

6 g that their role is not merely in refolding denatured protein.

7 were bound covalently to the native and heat denatured protein.

8 lexibility in more structured regions of the denatured protein.

9 TraR but only when SDS was included with the denatured protein.

10 energy of the transition between native and denatured protein.

11 assignments were to signals from inactive or denatured protein.

12 nally activated dissociation (CAD) MS of the denatured protein.

13 n full reduction and was not observed in the denatured protein.

14 nondenatured protein and not in that of the denatured protein.

15 tA and/or may stimulate proteolysis of toxic denatured protein.

16 rils in microorganisms and animals, and many denatured proteins.

17 elical structures in both short peptides and denatured proteins.

18 uced hsp60 function in binding and refolding denatured proteins.

19 hat perform a protective function by binding denatured proteins.

20 ndependent behavior of radii of gyration for denatured proteins.

21 ting that it forms large complexes with heat-denatured proteins.

22 scaling behavior of polymeric quantities for denatured proteins.

23 ilitate the folding of newly synthesized and denatured proteins.

24 inds uniquely to GPVI in ligand blots of SDS-denatured proteins.

25 s thermotolerance and reduces aggregation of denatured proteins.

26 tressed, probably due to the accumulation of denatured proteins.

27 rge measured by CE, Z(CE), of the folded and denatured proteins.

28 s thermotolerance and reduces aggregation of denatured proteins.

29 w stretches randomly coiled DNA molecules or denatured proteins.

30 ar proteins with known X-ray structure and 5 denatured proteins.

31 eading to suppression of aggregation by acid-denatured proteins.

32 e exposed hydrophobic regions of unfolded or denatured proteins.

33 and with fluorescence quenching studies with denatured proteins.

34 , Hsp104 does not prevent the aggregation of denatured proteins.

35 s; its role appears to be the degradation of denatured proteins.

36 peratures and suppressing the aggregation of denatured proteins.

37 spectrum similar to those of other thermally denatured proteins.

38 hanced the capacity of GroEL to bind to many denatured proteins.

39 o study submillisecond folding of chemically denatured proteins.

40 lso markedly reduced by the binding of large denatured proteins.

41 natured proteins are more expanded than heat-denatured proteins.

42 trypsin solution digestion of heat- or urea-denatured proteins.

43 the activity of chaperones that refold heat-denatured proteins.

44 gnificantly less than those calibrated using denatured proteins.

45 e and fold a wide range of nascent or stress-denatured proteins.

46 e diverse structural properties of 6 M GdmCl-denatured proteins.

47 ed as a probe of local mobility in partially denatured proteins.

48 an important role in determining the fate of denatured proteins.

49 all sizes are found within the interiors of denatured proteins.

50 t the folding of newly translated and stress-denatured proteins.

51 theoretical framework for describing highly denatured proteins.

52 aperone activity inhibits the degradation of denatured proteins.

53 at shock proteins, are involved in refolding denatured proteins.

54 ammaS translocates and degrades unfolded and denatured proteins.

55 iffer significantly for the peptides and the denatured proteins; 2), the fluorescence intensity at la

56 Reduced and denatured proteins (20 mug) from each group were separat

57 Heat-denatured protein 24 (p24) antigen is an inexpensive ass

58 Do highly denatured proteins adopt random coil configurations?

59 ly found in short amyloidogenic peptides and denatured protein aggregates.

60 small reduction of the fraction of the heat denatured protein aggregates.

61 SPs to change their confirmation and release denatured protein, allowing other molecular chaperones s

62 tivation of HRI in response to heat shock or denatured proteins also resulted in a similar blockage o

63 the chromophore forms de novo from purified denatured protein and is a first-order process, we concl

64 ition) signals the state of unfolding of the denatured protein and is determined by the denaturing co

65 ween the native protein and the aggregate of denatured protein and SDS.

66 e no correlation between the conformation of denatured protein and the release of individual peptides

67 changes, corresponding to the binding of the denatured protein and the subsequent refolding of multip

68 the function of sHSPs is to stabilize stress-denatured protein and then act cooperatively with other

69 structural analysis of interactions between denatured proteins and GroEL is essential for an underst

70 lex interactions between gelatinized starch, denatured proteins and lipids.

71 highly efficient in selectively recognizing denatured proteins and maintaining them in a soluble, fo

72 ier could include exposure to heme proteins, denatured proteins and other plasma constituents known t

73 orted values for nonspecific urea binding to denatured proteins and peptides, suggesting that the str

74 llin can act as chaperones binding partially denatured proteins and preventing further denaturation a

75 2S and 16S ribosomal RNA can fold chemically denatured proteins and reactivate heat-induced aggregate

76 hown to interact differently with chemically denatured proteins and their newly translated counterpar

77 of the primary protection/repair pathway for denatured proteins and thermotolerance expression in viv

78 red, owing to the spectral similarity of the denatured proteins and unordered structures.

79 tion activity, promoting the renaturation of denatured proteins, and preferential binding to denature

80 n prevent oxidation, restore the function of denatured proteins, and thus prevent aggregation.

81 It demonstrates that most 6 M GdmCl-denatured proteins are approximately fully denatured, bu

82 ually convincing experiments have shown that denatured proteins are biased toward specific conformati

83 the most probable transient loops formed in denatured proteins are comprised of 10 amino acids.

84 n a competitive manner and that the fates of denatured proteins are determined by the relative activi

85 mensions of the large majority of chemically denatured proteins are effectively indistinguishable fro

86 Denatured proteins are first focused and separated in a

87 g on the wavelength range and whether or not denatured proteins are included in the reference set, fi

88 f RNase Sa; 3), the I(F) differences for the denatured proteins are mirrored in the peptides, showing

89 he same time, NMR results indicate that cold-denatured proteins are more expanded than heat-denatured

90 in the proteins; 4) the I(F) values for the denatured proteins are more than 30% greater than for th

91 laboratories have shown that many 6 M GdmCl-denatured proteins are structurally heterogeneous and st

92 stages of protein refolding when chemically denatured proteins are transferred to native conditions.

93 predicted to remain above 3 kcal mol(-1) for denatured proteins as large as 900 residues.

94 may be exposed to aggregate-prone misfolded/denatured proteins as part of its normal function.

95 model for testing the common description of denatured proteins as structureless random coils.

96 ost the same hydrodynamic radius as the urea-denatured protein at pD 3.8.

97 rinsically disordered proteins (IDPs) and of denatured proteins based on nuclear magnetic resonance s

98 horesis could distinguish between native and denatured protein, based on the difference in electropho

99 These groups are more solvated in a denatured protein before folding than on the surface of

100 Refolding of the denatured protein by dilution with buffer of pH 7.5 does

101 rmediates were formed from the fully reduced denatured protein by oxidation with dithiothreitol, then

102 making it possible to release and refold SDS-denatured proteins by adding sufficient amounts of NIS,

103 of chymotryptic fragments from acetonitrile-denatured proteins by tandem mass spectrometry revealed

104 hanism is postulated for the reactivation of denatured proteins by thioredoxin.

105 We find that modeled denatured proteins can be best described as follows.

106 polymers in a good solvent and ensembles for denatured proteins can be modeled by ignoring all intera

107 er of in vitro studies have shown that large denatured proteins can bind to class II molecules, and t

108 imeric protein and the lower affinity of the denatured protein compared with type II collagen.

109 hemical derivatization of native and reduced/denatured protein confirmed the presence of a single int

110 ervations for both P(II) helix formation and denatured protein conformations are discussed.

111 ence for the radii of gyration of chemically denatured proteins containing 50-400 residues.

112 In contrast to refolding of a denatured protein, cotranslational folding is complicate

113 d polypeptides as well as to bind and refold denatured proteins during stress.

114 is unable to facilitate the refolding of two denatured proteins, E. coli alkaline phosphatase and mit

115 Stress-denatured proteins effectively compete with trimeric hHS

116 nd in vitro it suppresses the aggregation of denatured proteins efficiently.

117 allows us to quantify the dominant forces in denatured protein ensembles.

118 result indicates that the pore through which denatured proteins enter the proteolytic chamber must be

119 The thermally denatured proteins exposed different functional groups l

120 Some denatured proteins fold to their native structures in on

121 ods (free trypsin digestion of heat- or urea-denatured proteins) for 6-300 ng RAW 264.7 cell protein

122 pectively, to retrieve and reactivate stress-denatured proteins from aggregates.

123 (sHSP) family and has the ability to prevent denatured proteins from aggregating in vitro.

124 When denatured proteins from cancer cells treated with radiol

125 The dimensions of a denatured protein, fully reduced ribonuclease A (r-RNase

126 The acid-denatured protein has a significantly smaller hydrodynam

127 onformational heterogeneity of the 6 M GdmCl-denatured protein has significant implications for the f

128 ond dynamics of the native and the variously denatured proteins have three dynamic regimes.

129 When a denatured protein immersed in electrolyte is driven thro

130 ased on the assumption that the epsilon of a denatured protein in 6 M guanidine-HCl can be calculated

131 and have spectra very similar to that of the denatured protein in 8 M guanidine hydrochloride.

132 ly with other HSPs to renature the partially denatured protein in an ATP-dependent manner.

133 The results of modeling denatured protein in this manner reveal important sequen

134 rmans chaperonin (Ch-CPN), is able to refold denatured proteins in an ATP-dependent manner and is str

135 pendently facilitating the refolding of acid-denatured proteins in the bacterial periplasm, which lac

136 y making it unlikely that HSP16.5 sequesters denatured proteins in the cavity.

137 Content of acidic monosaccharides and denatured protein increased with increasing FG extractio

138 olded protein but 1.9 equiv of zinc ion from denatured protein, indicating different affinities for e

139 ng by EmrE is recovered after refolding this denatured protein into dodecylmaltoside detergent micell

140 Rapid dilution of chemically denatured protein into folding conditions in the presenc

141 particularly with regard to the insertion of denatured protein into lipid bilayers.

142 pectroscopy following transfer of chemically denatured protein into refolding conditions.

143 ClpX translocates this denatured protein into the proteolytic chamber of ClpP a

144 he highest intensity charge states (HICS) of denatured protein ions generated by electrospray ionizat

145 The hydrodynamic radius of the urea-denatured protein is much less sensitive to pH.

146 Thus, nativelike structure in the denatured protein is stabilized by the involvement of Tr

147 conclusion that the long-range structure of denatured proteins is encoded primarily by local steric

148 ment of this inherent dynamics in chemically denatured proteins is extremely challenging due to vario

149 en UPP-mediated degradation and refolding of denatured proteins is governed by relative levels of CHI

150 Detection of residual structure in denatured proteins is of interest because fleetingly str

151 However, a collapse of denatured proteins is revealed using atomistic molecular

152 trehalose also suppresses the aggregation of denatured proteins, maintaining them in a partially-fold

153 This denatured protein matrixes could be in part preventing s

154 the dynamic properties of Trp59 between each denatured protein may be direct evidence for a relative

155 Stress-denatured proteins may titer a limiting component of the

156 be used to detect the primary structure of a denatured protein molecule.

157 n is attributable to a weak association with denatured protein molecules and is therefore most likely

158 namic radii of the folded, unfolded and urea denatured protein molecules at pD 3.8 have been derived.

159 apid and efficient way of stretching DNA and denatured protein molecules for detection by fluorescenc

160 The urea-denatured protein monomers begin to aggregate as soon as

161 ctions for a large set of denatured peptide, denatured protein, native-like protein, and native-like

162 Indeed, it has been demonstrated that highly denatured proteins obey random-coil statistics.

163 droplet of sample solution containing DNA or denatured protein on a MgCl2-soaked mica surface.

164 zed both the native cAMP-PDEs as well as the denatured proteins on Western immunoblot analysis.

165 oxoid formulation consistently outperforms a denatured protein preparation in all of the metrics stud

166 e binds exposed hydrophobic surfaces of acid-denatured proteins, preventing their irreversible aggreg

167 sed to elevated temperatures (42 degrees C), denatured protein (reduced carboxymethylated bovine seru

168 and structural biologists studying how pure, denatured proteins refold spontaneously in the test tube

169 The detailed characterization of denatured proteins remains elusive due to their mobility

170 inclusion bodies must be solubilized and the denatured protein renatured if an active molecule is to

171 ischaemia, the accumulation of immature and denatured proteins results in ER dysfunction, but the up

172 Pressure-denatured proteins, unlike heat-denatured proteins, retain a compact structure with wate

173 icate that the dimensions of most chemically denatured proteins scale with polypeptide length by mean

174 It is generally believed that unfolded or denatured proteins show random-coil statistics and hence

175 than 50% greater in the peptides than in the denatured proteins, showing that long-range effects limi

176 tructure to induce significant compaction of denatured proteins, significantly affecting folding path

177 random coil has been the dominant model for denatured proteins since the 1950s, and it has long been

178 Denatured protein-sodium dodecyl sulfate (SDS) complexes

179 ained by subtracting spectra of unheated and denatured protein solutions at different temperature-tim

180 C1q, and not the collagen-like tail or heat-denatured protein, stimulated Mer expression.

181 digestion conditions and, by inference, from denatured protein structure.

182 more efficient in binding to and stabilizing denatured protein substrates compared with HSP70.

183 oposed based on in vitro studies: binding to denatured protein substrates, followed by their presenta

184 folding reaction increases upon binding with denatured protein substrates.

185 experimentally determined coil dimensions of denatured proteins successfully.

186 mediates the ATP-dependent refolding of heat-denatured proteins, such as firefly luciferase.

187 al protein folding and to target and degrade denatured proteins, suggesting that the accumulation of

188 In vitro refolding of the denatured protein takes place in the presence of dithiot

189 Improperly folded or denatured proteins tend to aggregate and accumulate in c

190 matrix may be enriched in, if not formed by, denatured proteins that function in pre-mRNA packaging,

191 ilability of realistic atomic models for the denatured protein, the common approach of using small pe

192 regation of unfolded polypeptides and refold denatured proteins, thereby remedying phenotypic effects

193 orce unfolding, and mediate threading of the denatured protein through the ClpX pore.

194 covery after severe stress by disaggregating denatured proteins through a poorly understood mechanism

195 olding of disulfide containing proteins from denatured protein to native protein involves numerous th

196 ular chaperones that interact with partially denatured proteins to prevent aggregation.

197 onomous chaperone and associates with stress-denatured proteins to prevent them from aggregation simi

198 quantity of Hsc70 binding substrates (e.g., denatured protein) to sequester Hsc70 and inhibit the ab

199 ing KL in Escherichia coli and refolding the denatured protein under conditions that promote the form

200 haracterizing the conformational ensemble of denatured proteins under folding conditions.

201 In the time series of folding, the denatured proteins undergo a conformational change towar

202 t that DegP and DegQ may degrade transiently denatured proteins, unfolded proteins which accumulate i

203 Pressure-denatured proteins, unlike heat-denatured proteins, reta

204 Radii of gyration of denatured proteins vary with chain length and are insens

205 tegy that promotes the folding of chemically denatured proteins via the sequential addition of low mo

206 The acid denatured protein was digested with pepsin and analyzed

207 found that optimal folding occurred when the denatured protein was diluted at 4 degrees C in approxim

208 ce in spin probe mobility between folded and denatured protein was marked, and in the folded protein,

209 The denatured protein was then refolded on the resin, and th

210 The secondary structure corresponding to the denatured proteins was approximated to be 90% unordered,

211 experimental values RG and RE For chemically denatured proteins we obtain mutual consistency in our i

212 o assay conformational preferences of highly denatured proteins, we quantify a variety of properties

213 ce data suitable for comparison with data of denatured proteins, we repeated the assignment in 7 M ur

214 The denatured proteins were used as substrate for tryptic hy

215 ng, affinity columns containing a variety of denatured proteins were used.

216 is reduced in the molten globule and in the denatured proteins when compared to that of the native p

217 ced UPP activity suppresses the refolding of denatured proteins whereas elevated chaperone activity i

218 eflect their cooperation as cochaperones for denatured proteins, whereas Hsp88 and Hsp30 may form a c

219 radius, 28.2A, compared to that of the urea-denatured protein, which is 33.6A at pD 3.8.

220 olding is typically initiated with 6 M GdmCl-denatured proteins, which are generally considered fully

221 ons with water determine whether a partially denatured protein will become more native-like under ref

222 Reactivity of native, reduced, and denatured protein with 4-pyridine disulfide and dithiobi

223 ion of chemical shifts in the spectra of the denatured protein with chemical shifts of sequenced pept

224 olabeled PPDK were generated by treating the denatured protein with trypsin or alpha-chymotrypsin.

225 f this remarkable promiscuity by mapping two denatured proteins with very different conformational pr

226 The observation that denatured proteins yield scaling exponents, nu, consiste