ライフサイエンスコーパス: guanidine hydrochloride

1 t the lowest denaturant concentration (0.2 M guanidine hydrochloride).

2 ce and circular dichroism in the presence of guanidine hydrochloride.

3 r during reactivation following unfolding in guanidine hydrochloride.

4 versibly denatured into unfolded monomers by guanidine hydrochloride.

5 ps comes from bulk-type solvation in the 6 M guanidine hydrochloride.

6 oinsulin following disulfide reassortment in guanidine hydrochloride.

7 in numbers while growing in the presence of guanidine hydrochloride.

8 pared to the complete unfolding caused by 6M guanidine hydrochloride.

9 histidine residues have been measured in 3 M guanidine hydrochloride.

10 its retention was not diminished by urea and guanidine hydrochloride.

11 nsitivity to the [PSI]-curing chemical agent guanidine hydrochloride.

12 heir thermodynamic stability by unfolding in guanidine hydrochloride.

13 ilar to that of the denatured protein in 8 M guanidine hydrochloride.

14 destabilization of apoA-I to denaturation by guanidine hydrochloride.

15 lexes are dissociated by SDS-PAGE and in 4 M guanidine hydrochloride.

16 displays a different sensitivity to urea and guanidine hydrochloride.

17 ould be titrated only in the presence of 8 M guanidine hydrochloride.

18 ight alpha-1,6 glucan or fully eluted by 4 M guanidine hydrochloride.

19 ltimers were solubilized into monomers using guanidine hydrochloride.

20 for the displacement of apo A-I from HDL by guanidine hydrochloride.

21 ained folded even at 120 degrees C or in 8 M guanidine hydrochloride.

22 asured in concentrated solutions of urea and guanidine hydrochloride.

23 itivity to the viral RNA synthesis inhibitor guanidine hydrochloride.

24 age of all membrane proteins, in contrast to guanidine hydrochloride.

25 lar mixture of the two isoforms denatured in guanidine hydrochloride.

26 multimeric structure was first disrupted by guanidine hydrochloride.

27 only slightly more tolerant to unfolding by guanidine hydrochloride.

28 ive boiling in sodium dodecyl sulfate or 5 M guanidine hydrochloride.

29 tudy the unfolding of the protein induced by guanidine hydrochloride.

30 their slow unfolding rate upon incubation in guanidine hydrochloride.

31 quired addition of a denaturant, such as 1 M guanidine-hydrochloride.

32 A solution containing 6M guanidine hydrochloride, 0.2% nondenaturing detergent, a

33 CaCl(2) +92.2, MgCl(2) +54.0, butanol +37.4, guanidine hydrochloride +31.9, urea +16.6, glycerol [> 6

34 ansfer reaction appears (4.0 x 10(6) s(-1), [guanidine hydrochloride] = 5.4 M) that is limited by the

35 As the protein is denatured with guanidine hydrochloride, a faster adiabatic electron-tra

36 nds in the presence of increasing amounts of guanidine hydrochloride and alkylation with [(12)C]iodoa

37 Plasma was extracted in the presence of guanidine hydrochloride and analysed by LC-MS/MS.

38 When native MG1 was placed in 4 M guanidine hydrochloride and chromatographed on Sepharose

39 Stability has been evaluated using guanidine hydrochloride and pH denaturation methods.

40 s solubilized from inclusion bodies with 6 M guanidine hydrochloride and purified by metal chelate af

41 16 heterodimer designs, denaturation in 5 M guanidine hydrochloride and reannealing-almost all of th

42 on and withstands even high concentration of guanidine hydrochloride and reducing agents.

43 from inclusion bodies has been denatured in guanidine hydrochloride and refolded and the characteris

44 be regained by denaturing the P1 dimer with guanidine hydrochloride and renaturing it by dialysis, s

45 e also resistant to chemical denaturation by guanidine hydrochloride and retain their secondary struc

46 cleral proteoglycans were extracted with 4 M guanidine hydrochloride and separated by molecular sieve

47 the millisecond scale with a mixture of 6 M guanidine hydrochloride and sodium borohydride, which st

48 Denaturation of AKe mutants by guanidine hydrochloride and subsequent refolding experim

49 f these mutants was assessed by unfolding in guanidine hydrochloride and thermal denaturation.

50 ns and monomeric controls were determined by guanidine hydrochloride and thermal denaturation.

51 the spectrum of human prion strains to both guanidine hydrochloride and thermal unfolding.

52 Treatment of Mia40 with guanidine hydrochloride and triscarboxyethylphosphine hy

53 Guanidine hydrochloride and urea both absorb strongly in

54 ifferences between the two proteins involved guanidine hydrochloride and urea denaturations monitored

55 the presence of the widely used denaturants guanidine hydrochloride and urea has only recently been

56 Similarly, guanidine hydrochloride and urea m-values are in good ag

57 Guanidine hydrochloride and urea-induced chemical denatu

58 on the unfolding and disassembly of GroEL in guanidine hydrochloride and urea.

59 are hypersensitive to curing of [PSI(+)] by guanidine-hydrochloride and partially cured of [PSI(+)]

60 the presence of denaturant (4 M urea or 2 M guanidine hydrochloride) and basic pH (8.0), reduced mPr

61 where dilute solutions of cyanoacetaldehyde, guanidine hydrochloride, and 0.5 M NaCl were evaporated

62 owever, the protein remains soluble in 0.4 M guanidine hydrochloride, and circular dichroism (CD) and

63 of pp65 with the NM resisted washes with 1 M guanidine hydrochloride, and direct binding to the NM co

64 protein, domain I of the intermediate at 2 M guanidine hydrochloride, and the unfolded state at 6 M o

65 The concentration of guanidine thiocyanate, guanidine hydrochloride, and urea required to denature 5

66 With guanidine hydrochloride as a denaturant, the classificat

67 However, with 6 M guanidine hydrochloride as the denaturant, the yield of

68 nmodified E-FABP to chemical denaturation by guanidine hydrochloride, as assessed by changes in intri

69 roteolysis, and by the apparent unfolding in guanidine hydrochloride, as detected by SE-HPLC.

70 from bovine heart following denaturation in guanidine hydrochloride, as well as following inactivati

71 particles was released after exposure to 4 M guanidine hydrochloride at 80 degrees C for 20 min.

72 We have demonstrated that an approach using guanidine hydrochloride at low concentrations to progres

73 ng the 24-mers into individual subunits with guanidine hydrochloride at pH 3.5, and renaturing to for

74 H33N/H26Q, and tuna wild type), unfolded in guanidine hydrochloride at pH 6.5, demonstrate that thes

75 xperiments of the proteins were performed in guanidine hydrochloride at pH 7.0, 37 degrees C, or urea

76 ore stably than natural core streptavidin in guanidine hydrochloride at very acidic pH.

77 ration column run in denaturing solvent (6 M guanidine hydrochloride) at the characteristic positions

78 Upon addition of guanidine hydrochloride, both mutants exhibit a fast con

79 of the purified enzyme at 4 degrees C in 6 M guanidine hydrochloride buffered at pH 7.0 in the presen

80 ET was retained in the presence of 0.6-1.0 m guanidine hydrochloride but was lost at higher concentra

81 egree, in formation of the molten globule in guanidine hydrochloride, but not in the complete unfoldi

82 wed a marked stabilization when denatured by guanidine hydrochloride, but showed significant destabil

83 s are dissociated during SDS-PAGE and by 4 M guanidine hydrochloride, but the released proteins appea

84 of the denatured state was determined in 3 M guanidine hydrochloride by evaluating the strength of he

85 orin that had been renatured from either 4 M guanidine hydrochloride by extensive dialysis or cooled

86 inate, cellulose sulfate, poly (methylene-co-guanidine) hydrochloride, calcium chloride, and sodium c

87 m unfolding of cytochrome c as a function of guanidine hydrochloride concentration at neutral pH.

88 the intrinsic fluorescence as a function of guanidine hydrochloride concentration helped confirm the

89 iscosity and refractive index changes as the guanidine hydrochloride concentration increases.

90 The dependence on guanidine hydrochloride concentration of both rates and

91 ght scattering measurements as a function of guanidine hydrochloride concentration.

92 of the Met80 heme ligand by histidine 73 at guanidine hydrochloride concentrations much lower than r

93 Even at guanidine hydrochloride concentrations well beyond the u

94 ation of loop formation probabilities in 3 M guanidine hydrochloride, conditions that fully denature

95 Titration of guanidine hydrochloride converts the higher order oligom

96 Cytochrome c, unfolded in guanidine hydrochloride/D2O, was allowed to refold in a

97 action extracted with 70% formic acid or 6 M guanidine hydrochloride decreased markedly in the cells

98 Furthermore, the addition of guanidine hydrochloride decreased, whereas the addition

99 ar protein, cytochrome c, in the presence of guanidine hydrochloride denaturant.

100 abilities of all variants were determined by guanidine hydrochloride denaturation and interaction ene

101 pproximately 25 kcal/mol) as investigated by guanidine hydrochloride denaturation curves monitored by

102 le both complexes showed virtually identical guanidine hydrochloride denaturation curves.

103 ype TTR exhibit analogous stability based on guanidine hydrochloride denaturation curves.

104 CD spectroscopy and guanidine hydrochloride denaturation demonstrate that th

105 on the folding stability of AR by FoldX and guanidine hydrochloride denaturation experiment, and fou

106 Guanidine hydrochloride denaturation experiments yielded

107 e, but showed significant destabilization to guanidine hydrochloride denaturation in the lipid-bound

108 comparable responses of both prion types to guanidine hydrochloride denaturation indicated this occu

109 protein species, characterized by different guanidine hydrochloride denaturation kinetics.

110 Guanidine hydrochloride denaturation leads to a shorter

111 n the triple mutant cycle were determined by guanidine hydrochloride denaturation methods and used to

112 Guanidine hydrochloride denaturation monitored by circul

113 Above pH 5, the m-values from guanidine hydrochloride denaturation of the WT and H73 v

114 he stability of the insertions as assayed by guanidine hydrochloride denaturation ranged from nearly

115 CD and guanidine hydrochloride denaturation results indicate th

116 Guanidine hydrochloride denaturation studies monitored b

117 G0 of unfolding of alpha t alpha measured by guanidine hydrochloride denaturation was determined to b

118 ties of these multiple mutants determined by guanidine hydrochloride denaturation were 3.4 to 5.6 kca

119 the protein, as measured both by thermal and guanidine hydrochloride denaturation.

120 Unfolding free energies were obtained by guanidine hydrochloride denaturation.

121 of these 58 mutant proteins were measured by guanidine hydrochloride denaturation.

122 bilities of these mutants were determined by guanidine hydrochloride denaturation.

123 rotein relative to wild type was measured by guanidine hydrochloride denaturation.

124 , and most clones tested were more stable to guanidine hydrochloride denaturation.

125 Guanidine hydrochloride denaturations in the presence of

126 Guanidine hydrochloride denaturations monitored by the c

127 Guanidine hydrochloride denaturations were performed to

128 An electronically excited Zn-porphyrin in guanidine hydrochloride denatured Zn-substituted cytochr

129 ns-to-heme distances resembling those in the guanidine hydrochloride-denatured state.

130 Guanidine hydrochloride-denatured UvrA was reactivated b

131 The guanidine hydrochloride dependence of the alkaline confo

132 ation profile of the protein, treatment with guanidine hydrochloride did not.

133 d native-like, the radius in the presence of guanidine hydrochloride falls well within the range expe

134 6.0 M urea or by treatment with 4.0 to 6.0 M guanidine hydrochloride for 24 h at 4 degrees C.

135 histidine-heme loop has been measured in 3 M guanidine hydrochloride for all variants.

136 has been studied following unfolding in 6 m guanidine hydrochloride for different periods of time.

137 was studied by destabilizing the protein in guanidine hydrochloride (GdHCl) or urea, pulse-labeling

138 ed with low, nondenaturing concentrations of guanidine hydrochloride (GdmHCl) foster disaggregation a

139 ntrations were tested in the presence of 1 M guanidine hydrochloride (Gdn), at pH values ranging from

140 experimental probes under native (0 M NaCl, guanidine hydrochloride (Gdn-HCl)), moderately destabili

141 ct forms of these proteins were denatured in guanidine hydrochloride (Gdn.HCl) and then refolded by d

142 mational-stability assays, we determined the guanidine hydrochloride (Gdn.HCl) concentration required

143 a systematic investigation of the effect of guanidine hydrochloride (Gdn.HCl)-induced structural per

144 (D-LDH) of Escherichia coli by a denaturant, guanidine hydrochloride (Gdn.HCl).

145 To fill this gap, we studied the effects of guanidine hydrochloride (GdnHCl) and heating on PrP(Sc)

146 streptococcal protein G (GB1) was induced by guanidine hydrochloride (GdnHCl) and studied by circular

147 loop formation are measured as a function of guanidine hydrochloride (GdnHCl) concentration for loop

148 ways of transthyretin (TTR) as a function of guanidine hydrochloride (GdnHCl) concentration.

149 chia coli alkaline phosphatase (AP) from the guanidine hydrochloride (GdnHCl) denatured state is char

150 structure of cytochrome c through the pH and guanidine hydrochloride (gdnHCl) dependence of the His 7

151 orylation on the conformational stability by guanidine hydrochloride (GdnHCl) dependent denaturation

152 10 to 100 micromolar concentration range by guanidine hydrochloride (GdnHCl) is well modeled as a tw

153 circular dichroism (CD) in conjunction with guanidine hydrochloride (GdnHCl) jump stopped-flow CD ex

154 The guanidine hydrochloride (GdnHCl) mediated denaturation p

155 s provide further insight into the effect of guanidine hydrochloride (GdnHCl) on Sup35 aggregates.

156 utase (SOD1) dimers induced by the chaotrope guanidine hydrochloride (GdnHCl) or the reductant Tris(2

157 required PrPC or rPrP to be destabilized by guanidine hydrochloride (GdnHCl) or urea and PrP(90-145)

158 d by the loss of proteinase K resistance) by guanidine hydrochloride (GdnHCl) resulted in decreased i

159 It has been shown that with urea and guanidine hydrochloride (GdnHCl) some proteins exhibit d

160 staphylococcal nuclease (SN) denaturation in guanidine hydrochloride (GdnHCl) to test whether GdnHCl-

161 pB exhibited a biphasic unfolding trend upon guanidine hydrochloride (GdnHCl) treatment and underwent

162 PrP(Sc) solubilized with 5 m guanidine hydrochloride (GdnHCl) was unfolded to a predo

163 sozyme) in the presence and absence of 1.0 m guanidine hydrochloride (GdnHCl) were investigated by me

164 places chaotropic reagents, such as urea and guanidine hydrochloride (GdnHCl) with an acid labile sur

165 Guanidine hydrochloride (GdnHCl), a strong chaotropic ag

166 n buffers with specific amounts of glycerol, guanidine hydrochloride (GdnHCl), and sodium chloride (N

167 wth in the presence of low concentrations of guanidine hydrochloride (GdnHCl), leading to the generat

168 ontinuously with increasing concentration of guanidine hydrochloride (GdnHCl), the F(ab')2 fragment o

169 ity of PrP(Sc) as determined by unfolding in guanidine hydrochloride (GdnHCl), which is tightly and p

170 dependent of nondenaturing concentrations of guanidine hydrochloride (GdnHCl).

171 ies, and was subsequently solubilized in 8 M guanidine hydrochloride (GdnHCl).

172 is inhibited by millimolar concentrations of guanidine hydrochloride (GdnHCl).

173 d K273A, were mixed in low concentrations of guanidine hydrochloride (GdnHCl).

174 ranging from 22 to 46 in 1.5, 3.0, and 6.0 M guanidine hydrochloride (GdnHCl).

175 ter solutions, with chemical denaturation by guanidine hydrochloride (GdnHCl).

176 er varying denaturing conditions (2 M to 6 M guanidine hydrochloride, gdnHCl).

177 Guanidine hydrochloride (GnHCl) denaturation of I92E and

178 Under denaturing conditions (urea, guanidine hydrochloride, guanidine thiocyanate, organic

179 has been denatured in the presence of urea, guanidine hydrochloride, guanidine thiocyanate, organic

180 ity of these viral products to inhibition by guanidine hydrochloride (GuHCl) (which targets minus-str

181 chain variable domain SMA in the presence of guanidine hydrochloride (GuHCl) and characterized their

182 rmined some effects of low concentrations of guanidine hydrochloride (GuHCl) and of urea on functiona

183 s monitored during solvent denaturation with guanidine hydrochloride (GuHCl) and was used to calculat

184 Millimolar concentrations of guanidine hydrochloride (GuHCl) are known to inhibit the

185 ferricytochrome c titrated with 2.3 to 4.6 M guanidine hydrochloride (GuHCL) at pH 7 and 40 degrees C

186 an der Waals interactions in the presence of guanidine hydrochloride (GuHCl) but also because of its

187 r capsulatus were performed as a function of guanidine hydrochloride (GuHCl) concentration in the abs

188 Guanidine hydrochloride (GuHCl) denaturation studies rev

189 ction of 104 mutant proteins was analyzed by guanidine hydrochloride (GuHCl) denaturation, using intr

190 asuring their structural stabilities through guanidine hydrochloride (GuHCl) denaturation.

191 Guanidine hydrochloride (GuHCl) dissociation of the P3 s

192 embly of the virus capsid in the presence of guanidine hydrochloride (GuHCl) exhibits strong hysteres

193 unfolding of bovine serum albumin (BSA) with guanidine hydrochloride (GuHCl) has been investigated us

194 Low concentrations of guanidine hydrochloride (GuHCl) increase the rate (and t

195 more complex when the highly chaotropic salt guanidine hydrochloride (GuHCl) is employed.

196 The unfolding of each protein in 5.4 M guanidine hydrochloride (GuHCl) is well described as a t

197 acy of three sample preparation methods [6 M guanidine hydrochloride (GuHCl) protein extraction + in-

198 lectron transfer to unfolded Fe(III)cyt c in guanidine hydrochloride (GuHCl) solutions.

199 Upon addition of the chemical denaturant guanidine hydrochloride (GuHCl) to dfx, a reversible flu

200 Mucins were extracted in guanidine hydrochloride (GuHCl) with protease inhibitors

201 In increasing levels of guanidine hydrochloride (GuHCl), a sharp red shift in fl

202 Below 2.0 M guanidine hydrochloride (GuHCl), a species of N-PGK (den

203 ed unfolded-state dimensions from 1.4 to 5 M guanidine hydrochloride (GuHCl), and by smFRET (at 25 de

204 aturants sodium dodecyl sulfate (SDS), urea, guanidine hydrochloride (GuHCl), and trifluoroacetic aci

205 or; these distributions demonstrate that the guanidine hydrochloride (GuHCl)-denatured polypeptide en

206 cantly increased the resistance to urea- and guanidine hydrochloride (GuHCl)-induced denaturation, ox

207 denaturing the mAb in the presence of NEM in guanidine hydrochloride (GuHCl).

208 be moderately populated in approximately 2 M guanidine hydrochloride (GuHCl).

209 the addition of low concentrations of added guanidine hydrochloride (GuHCl).

210 he refolding of the protein denatured in 6 M guanidine hydrochloride (GuHCl).

211 case of two different denaturants, urea and guanidine hydrochloride (GuHCl).

212 (C), primarily using the chemical denaturant guanidine hydrochloride (GuHCl).

213 c bacterium Thermus thermophilus, induced by guanidine hydrochloride (GuHCl)1 at different temperatur

214 quilibrium, under denaturing conditions (3 M guanidine hydrochloride), has been measured by pH titrat

215 In 1.1 M guanidine hydrochloride, however, the effective hydrodyn

216 The unfolding forces determined in 1 M guanidine hydrochloride indicate that in these condition

217 pparent pK(a) for His 26-heme binding in 3 M guanidine hydrochloride indicates that the P25A mutation

218 e the same in the presence or absence of 6 M guanidine hydrochloride, indicating that the native and

219 ormational status within the amyloid form in guanidine hydrochloride-induced denaturation experiments

220 Guanidine hydrochloride-induced denaturation Gibbs energ

221 Guanidine hydrochloride-induced denaturation studies rev

222 and characterized the thermally induced and guanidine hydrochloride-induced denaturation transitions

223 Guanidine hydrochloride-induced denaturation was used to

224 ated by site-directed mutagenesis, kinetics, guanidine hydrochloride-induced denaturation, and nuclea

225 hat of the WT by 1.0 kcal/mol as measured by guanidine hydrochloride-induced denaturation.

226 Guanidine hydrochloride-induced equilibrium unfolding of

227 Guanidine hydrochloride-induced extension of the substra

228 The guanidine hydrochloride-induced unfolding transition sho

229 ltiple folding pathways, we investigated the guanidine hydrochloride-induced unfolding, conformationa

230 protein significantly, nor its resistance to guanidine hydrochloride-induced unfolding.

231 roism and visible absorbance measurements of guanidine-hydrochloride-induced disassembly of methemogl

232 the energetics of unfolding, we studied the guanidine-hydrochloride-induced unfolding and refolding

233 H and AMSH-LP are nearly identical; however, guanidine-hydrochloride-induced unfolding studies show t

234 [2-(alpha-hydroxybenzyl)-benzimidazole], and guanidine hydrochloride inhibit 2C ATPase activity.

235 Chemical denaturation by guanidine hydrochloride is also cooperative with a delta

236 The thermodynamics of unfolding by guanidine hydrochloride is also reported.

237 C and (b) a strong chaotropic agent, such as guanidine hydrochloride, is critical for preventing loss

238 Guanidine hydrochloride m values of 1.67 +/- 0.08 and 1.

239 yvinyl alcohol and polyvinyl pyrrolidone) or guanidine hydrochloride (negative control).

240 en 7 and 5, the unfolding of hPrP(90-231) in guanidine hydrochloride occurs as a two-state transition

241 The effect of pH and concentration of guanidine hydrochloride on the rate of synthesis and yie

242 mationally more stable following exposure to guanidine hydrochloride or Sarkosyl than was RML PrP27-3

243 he denatured state in the presence of either guanidine hydrochloride or urea was monitored by the spi

244 a function of the chemical denaturant (e.g., guanidine hydrochloride or urea) concentration.

245 nificantly altered by the presence of either guanidine hydrochloride or urea.

246 e pyrimidine yields are much lower than with guanidine hydrochloride or urea.

247 oism spectra of cytochrome c (cytc) in 4.6 M guanidine hydrochloride (pH 6.5) indicate that the secon

248 roism (CD) at 222 and 275 nm at 0.9 or 2.6 M guanidine hydrochloride, pH 7.0, and 5 degrees C.

249 nt in inclusion bodies, was solubilized with guanidine hydrochloride, renatured, and purified by DEAE

250 We serendipitously discovered that guanidine hydrochloride rescues septin function in cdc10

251 Thus, chemical rescue of R57G by guanidine hydrochloride restores many but not all wild-t

252 dehydrogenase-depleted adult A. suum PDC in guanidine hydrochloride resulted in two E3-depleted E2 c

253 H463F and Y74F Trpase after unfolding in 4 M guanidine hydrochloride results in a dramatic increase i

254 ow) in the presence of low concentrations of guanidine hydrochloride results in a transition to PrP(S

255 he unfolding of lysozyme with either urea or guanidine hydrochloride results in different phasor traj

256 ic studies on His-heme loop formation in 3 M guanidine hydrochloride reveal significant stabilization

257 The folding rates at 0 M guanidine hydrochloride show a non-Arrhenius temperature

258 Treatment of the secreted toxin with guanidine hydrochloride significantly restored cytolytic

259 eparin chromatography after refolding of the guanidine hydrochloride solubilized protein.

260 ynamics when Monellin was denatured in a 6 M guanidine hydrochloride solution and obtained a totally

261 eased in the wild-type samples by applying a guanidine hydrochloride solution at pH 9.5 and in the D9

262 effects of viscosity and refractive index of guanidine hydrochloride solutions to calibrate FCS data.

263 ro after denaturation by high temperature or guanidine hydrochloride solutions.

264 ransfer to unfolded Fe(III)cyt b562 in 2-3 M guanidine hydrochloride solutions.

265 ues of delta GN-->U,25 derived from urea and guanidine hydrochloride studies allowed an estimation of

266 Titration of halothane binding with guanidine hydrochloride suggested more protection of bin

267 P41 at significantly lower concentrations of guanidine hydrochloride than for P46, are further eviden

268 On the addition of 2.2 M guanidine hydrochloride the effective hydrodynamic radiu

269 nt biglycan was disrupted by exposure to 4 M guanidine hydrochloride, the affinity for collagen type

270 At 0.3 M guanidine hydrochloride, the entire transition from nati

271 ( T(m) ~ 75 degrees C) or denatured by 1.5 M guanidine hydrochloride, the Ico8 cages remained folded

272 The folding rates increase with decreasing guanidine hydrochloride; the extrapolated time constant

273 126 mM NAD+ for 3 h, followed by dilution of guanidine hydrochloride to 0.18 M and of NAD+ to 0.076 m

274 he protease site with trypsin, denaturing in guanidine hydrochloride to disrupt the complex, separati

275 By using the strong protein denaturant 8 M guanidine hydrochloride to solubilize the fibers, we dem

276 more efficient than wt protein in refolding guanidine hydrochloride-treated malate dehydrogenase to

277 insensitivity of the intrinsic viscosity to guanidine hydrochloride treatment all suggest that LigBC

278 of cholesteryl ester transfer protein or by guanidine hydrochloride treatment, a fraction of apoA-I,

279 [SW+] can be eliminated by guanidine hydrochloride treatment, HSP104 deletion or lo

280 We find that, while the dimensions of the guanidine hydrochloride -unfolded molecule generally coi

281 between five residue pairs in the protein's guanidine hydrochloride-unfolded and trifluoroethanol-un

282 Guanidine hydrochloride unfolding transitions for the se

283 bovine cytochrome c is induced to unfold by guanidine hydrochloride via a stepwise mechanism, but it

284 with progressively higher concentrations of guanidine hydrochloride was correlated with a loss of ce

285 unfolding over an attainable pressure range, guanidine hydrochloride was employed.

286 tability since (i) the same concentration of guanidine hydrochloride was required for 50% unfolding,

287 ate of recombinant human IFN-gamma in 0.45 M guanidine hydrochloride was studied as a function of suc

288 The effect of pH on the denatured state (3 M guanidine hydrochloride) was evaluated with fluorescence

289 lding of proteins by the chemical denaturant guanidine hydrochloride, we have measured helix unfoldin

290 Urea and guanidine hydrochloride were ineffective at inducing thi

291 elevated temperatures and a chaotropic agent guanidine hydrochloride, were studied.

292 In 3 M guanidine hydrochloride, which disrupts apo A-II seconda

293 The best rescue agent is guanidine hydrochloride, which enhances the rate of the

294 rom the coupling of alcohols and benzamidine/guanidine hydrochloride with a maximum isolated yield of

295 The reaction of guanidine hydrochloride with cyanoacetaldehyde gives hig