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 r during reactivation following unfolding in guanidine hydrochloride.

3 versibly denatured into unfolded monomers by guanidine hydrochloride.

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

5 oinsulin following disulfide reassortment in guanidine hydrochloride.

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

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

8 heir thermodynamic stability by unfolding in guanidine hydrochloride.

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

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

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

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

13 ltimers were solubilized into monomers using guanidine hydrochloride.

14 displays a different sensitivity to urea and guanidine hydrochloride.

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

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

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

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

19 asured in concentrated solutions of urea and guanidine hydrochloride.

20 itivity to the viral RNA synthesis inhibitor guanidine hydrochloride.

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

22 multimeric structure was first disrupted by guanidine hydrochloride.

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

24 only slightly more tolerant to unfolding by guanidine hydrochloride.

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

26 their slow unfolding rate upon incubation in guanidine hydrochloride.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

47 Treatment of Mia40 with guanidine hydrochloride and triscarboxyethylphosphine hy

48 Guanidine hydrochloride and urea both absorb strongly in

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

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

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

52 Guanidine hydrochloride and urea-induced chemical denatu

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

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

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

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

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

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

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

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

61 With guanidine hydrochloride as a denaturant, the classificat

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

85 The dependence on guanidine hydrochloride concentration of both rates and

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

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

88 Even at guanidine hydrochloride concentrations well beyond the u

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

90 Titration of guanidine hydrochloride converts the higher order oligom

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

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

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

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

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

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

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

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

99 CD spectroscopy and guanidine hydrochloride denaturation demonstrate that th

100 Guanidine hydrochloride denaturation experiments yielded

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

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

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

104 Guanidine hydrochloride denaturation leads to a shorter

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

106 Guanidine hydrochloride denaturation monitored by circul

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

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

109 CD and guanidine hydrochloride denaturation results indicate th

110 Guanidine hydrochloride denaturation studies monitored b

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

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

113 Unfolding free energies were obtained by guanidine hydrochloride denaturation.

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

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

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

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

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

119 Guanidine hydrochloride denaturations in the presence of

120 Guanidine hydrochloride denaturations monitored by the c

121 Guanidine hydrochloride denaturations were performed to

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

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

124 Guanidine hydrochloride-denatured UvrA was reactivated b

125 The guanidine hydrochloride dependence of the alkaline confo

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

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

128 6.0 M urea or by treatment with 4.0 to 6.0 M guanidine hydrochloride for 24 h at 4 degrees C.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

146 10 to 100 micromolar concentration range by guanidine hydrochloride (GdnHCl) is well modeled as a tw

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

148 The guanidine hydrochloride (GdnHCl) mediated denaturation p

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

169 Guanidine hydrochloride (GnHCl) denaturation of I92E and

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

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

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

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

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

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

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

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

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

179 Guanidine hydrochloride (GuHCl) denaturation studies rev

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

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

182 Guanidine hydrochloride (GuHCl) dissociation of the P3 s

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

209 Guanidine hydrochloride-induced denaturation Gibbs energ

210 Guanidine hydrochloride-induced denaturation studies rev

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

212 Guanidine hydrochloride-induced denaturation was used to

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

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

215 Guanidine hydrochloride-induced equilibrium unfolding of

216 Guanidine hydrochloride-induced extension of the substra

217 The guanidine hydrochloride-induced unfolding transition sho

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

257 126 mM NAD+ for 3 h, followed by dilution of guanidine hydrochloride to 0.18 M and of NAD+ to 0.076 m

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

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

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

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

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

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

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

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

266 Guanidine hydrochloride unfolding transitions for the se

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

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

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

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

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

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

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

274 Urea and guanidine hydrochloride were ineffective at inducing thi

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

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

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

278 The reaction of guanidine hydrochloride with cyanoacetaldehyde gives hig