ライフサイエンスコーパス: RNase A

1 RNase A can be made toxic to cancer cells by replacing G

2 RNase A has a thermal pretransition near 320 K.

3 RNase A is a far more efficient catalyst of RNA cleavage

4 RNase A is so resistant to urea denaturation at pH* 6.35

5 RNase A is the prototype of an extensive family of diver

6 RNase A treatment of cellular chromatin released a fract

7 RNase A variants and homologues, such as G88R RNase A, t

8 RNase A, a model protein for oxidative folding studies,

9 RNase A-2, the more cationic (pI 11.0), is both angiogen

10 es [30-75] is similar to that of des [40-95] RNase A, in that des [30-75] ONC is also a disulfide-sec

11 ng of both bovine pancreatic ribonuclease A (RNase A) and a 58-72 fragment thereof from the fully red

12 rinogen), including enzymes (ribonuclease A (RNase A) and alkaline phosphatase).

13 ovalent interactions between ribonuclease A (RNase A) and cytidylic acid ligands (2'-CMP, CTP), a wel

14 Using ribonuclease A (RNase A) and saporin as two representative cytotoxic pro

15 Ribonuclease A (RNase A) and the ribonuclease inhibitor protein (RI) for

16 nd motions in wild-type (WT) Ribonuclease A (RNase A) are modulated by histidine 48.

17 Ribonuclease A (RNase A) can make multiple contacts with an RNA substrat

18 at divalent anion binding to ribonuclease A (RNase A) contributes to RNase A folding and stability.

19 ferent schemes to immobilize ribonuclease A (RNase A) in either a preferred orientation or random ori

20 The ribonuclease A (RNase A) superfamily has been the subject of extensive s

21 enin (hANG), a member of the ribonuclease A (RNase A) superfamily known to be involved in neovascular

22 onally varied members of the ribonuclease A (RNase A) superfamily provide an excellent opportunity to

23 ber of the bovine pancreatic ribonuclease A (RNase A) superfamily, is in phase III clinical trials as

24 , a protein belonging to the ribonuclease A (RNase A) superfamily, which has recently been found to h

25 Ribonuclease A (RNase A) undergoes more rapid conformational folding wit

26 lations of bovine pancreatic ribonuclease A (RNase A) up to its melting temperature (Tm approximately

27 The evolution of the ribonuclease A (RNase A) vertebrate-specific enzyme family is interestin

28 ppAp) with bovine pancreatic ribonuclease A (RNase A) was characterized by calorimetry and solution N

29 on of enzymatic product from ribonuclease A (RNase A) was investigated by creation of a chimeric enzy

30 single-turnover kinetics of ribonuclease A (RNase A) was measured with better than millisecond resol

31 d-type mice generated CML on ribonuclease A (RNase A), a model protein, by a pathway that required L-

32 th that of the parent enzyme ribonuclease A (RNase A), and a model was devised to assess the importan

33 homologue, bovine pancreatic ribonuclease A (RNase A), has been isolated and characterized.

34 conase (ONC), a homologue of ribonuclease A (RNase A), is in clinical trials for the treatment of can

35 id third domain (OMTKY3) and ribonuclease A (RNase A).

36 ynamics of bovine pancreatic ribonuclease A (RNase A).

37 d unfolded bovine pancreatic ribonuclease A (RNase A).

38 ONC is a homolog of ribonuclease A (RNase A).

39 ering hyaluronic acid (HA)-modified RNase A (RNase A-HA) in nanocomplex with cationic lipid-like mole

40 nto low-molecular-weight (LMW) species after RNase A treatment.

41 ) is a potent inducer of angiogenesis and an RNase A homologue whose ribonucleolytic activity is esse

42 In contrast, bovine RI binds to RNase 1 and RNase A with nearly equal affinity.

43 udies were performed on both apo RNase A and RNase A/pTppAp as a function of temperature.

44 ents, did not differ between apo RNase A and RNase A/pTppAp indicating that backbone dynamics contrib

45 s, electrophoretic mobility shift assay, and RNase A footprinting.

46 on for only two of the tracers: cytosine and RNase A.

47 of paromomycin binding on both RNase H- and RNase A-mediated cleavage of the RNA strand in the DNA.R

48 RNA hybrid duplex inhibits both RNase H- and RNase A-mediated cleavage of the RNA strand.

49 ipitation of hnRNPK and XRN2 from intact and RNase A-treated nuclear extracts followed by shotgun mas

50 Based on the simulations of OMTKY3 and RNase A, the current work has demonstrated the capabilit

51 ces in the folding mechanism between ONC and RNase A are attributed to the differences in their amino

52 The toxicity of ONC and RNase A variants relies on their ability to evade the cy

53 proteins of the ribonuclease family, ONC and RNase A, which have similar three-dimensional folds but

54 urifies with RNA as an inactive protein, and RNase A treatment enables strong DNA deaminase activity.

55 ucture of the complex between porcine RI and RNase A. hRI, which is anionic, also appears to use its

56 extent human pancreatic RNase (hPR), another RNase A superfamily member, activates human dendritic ce

57 ing sites were introduced throughout an anti-RNase A antibody interface.

58 Structure analysis of the original antibody-RNase A complex suggested peripheral interface residues

59 ics measurements, did not differ between apo RNase A and RNase A/pTppAp indicating that backbone dyna

60 elaxation studies were performed on both apo RNase A and RNase A/pTppAp as a function of temperature.

61 11.0), is both angiogenic and bactericidal; RNase A-1 (pI 10.2) has neither activity.

62 ntrast, the non-covalent interaction between RNase A and RI is one of the strongest known, with the R

63 tested (C408W, G410W, and C408W/G410W) bind RNase A with almost the same avidity as WT RI.

64 , although probably smaller than for binding RNase A and Ang.

65 For both RNase A(ECP) and H48A there is a 10-fold decrease in the

66 In both RNase A and angiogenin, only six residues appeared to be

67 differences between human RNase 1 and bovine RNase A.

68 aracteristics of aqueous solutions of bovine RNase A in the presence of 100 mM KCl and 10 mM Bis-Tris

69 inual comparisons of human RNase 1 to bovine RNase A, an enzyme that appears to function primarily in

70 hysicochemical constraints upon catalysis by RNase A, the effects of salt concentration, pH, solvent

71 sistent with the binding of two chlorides by RNase A.

72 indicates that catalysis of RNA cleavage by RNase A is limited by the rate of substrate association,

73 NA in the VSV nucleocapsid can be removed by RNase A, in contrast to what was previously reported.

74 oil region and the digestion of 7SK snRNA by RNase A treatment prevent this oligomerization.

75 The chimera (RNase A(ECP)) experiences only local perturbations in NM

76 ddition of TMAO to urea solutions containing RNase A also suppresses HX rate constants.

77 ional molecular units are formed from a core RNase A domain and a swapped complementary domain.

78 ould alter the course of disease, we created RNase A transgenic (Tg) mice.

79 Most importantly, free and RI-bound DEF-RNase A have pKa values of 6.68 and 7.29, respectively,

80 Using DEF-RNase A rather than fluorescein-RNase A in a microplate

81 ogether, this work characterizes a divergent RNase A ribonuclease with a unique expression pattern an

82 bonuclease (RNase) of the highly diversified RNase A superfamily.

83 deliver payloads of cytotoxic protein (i.e., RNase A) to the cells without a loss in its biological f

84 like fibril of the well-characterized enzyme RNase A contains native-like molecules capable of enzyma

85 ogues of the pancreatic ribonuclease family: RNase A and eosinophil cationic protein (or RNase 3).

86 on and function of RNase 7, one of the final RNase A superfamily ribonucleases identified in the huma

87 Free and RI-bound fluorescein-RNase A have pKa values of 6.35 and 6.70, respectively,

88 Using DEF-RNase A rather than fluorescein-RNase A in a microplate assay at pH 7.12 increased the Z

89 The average order parameter, S(2), for RNase A is 0.910 +/- 0.051.

90 ameters, S(2), were significantly higher for RNase A/pTppAp than for the apo enzyme indicating a decr

91 roup, and nonbridging phosphoryl oxygens for RNase A to values observed for hydronium- or hydroxide-c

92 and the results were compared with those for RNase A.

93 The K(i) value for RNase A is increased by a factor of >10(8), from 36 fM t

94 (Thr35, Asp67, and Phe98) are conserved from RNase A and serve to generate a similar bell-shaped pH v

95 se of their unglycosylated counterparts from RNase A.

96 s comparing unmodified peptides derived from RNase A and BID BH3 with various i,i+4 and i,i+7 stapled

97 reatic ribonuclease B (RNase B) differs from RNase A by the presence of an oligosaccharide moiety cov

98 ptide constructs based on the C peptide from RNase A, the conformational entropy is calculated versus

99 Removal of Tyr92 from RNase A resulted in the relatively rapid reduction of th

100 Nase A variants and homologues, such as G88R RNase A, that retain ribonucleolytic activity in the pre

101 In contrast, K7A/G88R RNase A is nearly 10-fold more cytotoxic than G88R RNase

102 complex of RI with fluorescein-labeled G88R RNase A was determined to be (7.5 +/- 0.4) x 10(-3) s(-1

103 A is nearly 10-fold more cytotoxic than G88R RNase A and has more than 10-fold less affinity for RI.

104 eater affinity than to the bovine homologue (RNase A).

105 in the reductive unfolding of the homologue, RNase A, there are two intermediates, arising from the r

106 d conformational changes are not observed if RNase A is allowed to equilibrate under denaturing condi

107 Immunoreactive RNases A-1 and A-2 (both approximately 16 kDa) were dete

108 In RNase A the average absolute errors for the carboxyl and

109 ein (ECP), replaced the 12-residue loop 1 in RNase A.

110 istidine residues (His12, -105, and -119) in RNase A were successfully determined by this method and

111 esidues around the (40-95) disulfide bond in RNase A, which is analogous to the (30-75) disulfide bon

112 m the (40-95) and (65-72) disulfide bonds in RNase A and the fourfold more exposed cysteine sulfur at

113 ents were used to compare mus-ms dynamics in RNase A in the apo form and as complexed to the substrat

114 t role in coordinating the dynamic events in RNase A.

115 indicating the importance of flexibility in RNase A in the overall rate-limiting product release ste

116 curves show that the time scale of motion in RNase A is unchanged when pTppAp binds and is similar to

117 LC-MS/MS to sequence the oligonucleotides in RNase A digests.

118 Mutation of Tyr92 to Phe92 in RNase A has no effect on its reductive unfolding pathway

119 er, a comparison of the critical residues in RNase A and human angiogenin, which share only 35% amino

120 Twenty-three of the 124 residues in RNase A were found to be intolerant to substitution with

121 However, 28 of the amino acid residues in RNase A were identified as undergoing chemical exchange

122 ion of the structured des [40-95] species in RNase A.

123 hat is integral in the rate-limiting step in RNase A enzyme function.

124 RNase 9, a catalytically inactive RNase A family member of unknown function, is expressed

125 ep of select ER-processed proteins including RNase A.

126 ase folding intermediate of disulfide-intact RNase A.

127 for two protein-ligand binding interactions (RNase A + cytidine 2'-monophosphate and streptavidin + b

128 Aminoacyl-tRNA synthetase binding is RNase A sensitive, whereas interaction with Mcm2-7 is nu

129 hil ribonuclease cluster, and the only known RNase A ribonuclease expressed specifically in response

130 nsity that occurs when a fluorescein-labeled RNase A binds to RI.

131 omatography-mass spectrometry (LC-MS) to map RNase A and T1 digestion products onto the tRNA, and use

132 his delivering hyaluronic acid (HA)-modified RNase A (RNase A-HA) in nanocomplex with cationic lipid-

133 results suggest that brain ribonuclease, not RNase A, is the true bovine homolog of human RNase 1, an

134 acids 71-76) and III (amino acids 89-104) of RNase A-2 are both important for bactericidal activity.

135 reveal that the side-chain of tyrosine 92 of RNase A, a highly conserved residue among mammalian panc

136 and HIV-1 Gag in the presence and absence of RNase A indicated that the two proteins do not interact

137 as no impact on the bactericidal activity of RNase A-2.

138 of DeltaG(HX) as a basis for HX analysis of RNase A urea denaturation is invalid.

139 activity that has been observed in assays of RNase A at low salt concentration.

140 revious studies showed that tight binding of RNase A and angiogenin (Ang) is achieved primarily throu

141 The conjugation of RNase A with 4-nitrophenyl 4-(4,4,5,5-tetramethyl-1,3,2-

142 The chemical conjugation of RNase A with HA both increased the supramolecular intera

143 r ROS, thereby restoring the cytotoxicity of RNase A for cancer therapy.

144 gradation does not limit the cytotoxicity of RNase A variants.

145 Thus, RI constrains the cytotoxicity of RNase A.

146 g molecules in the two-disulfide ensemble of RNase A.

147 olarized cells have diminished expression of RNase A superfamily proteins, and we report for the firs

148 25 degrees C during the oxidative folding of RNase A, are well characterized.

149 ] disulfide bond in the oxidative folding of RNase A, use has been made of [C65S, C72S], a three-disu

150 d PDI and reconstituted oxidative folding of RNase A.

151 Thus, the unfolded reduced forms of RNase A are not statistical coils with a more condensed

152 propensity of the unfolded reduced forms of RNase A to form the native set of disulfides directly, c

153 1.2 kcal/mol for the apo and pTppAp forms of RNase A, respectively.

154 92-Pro93 and Asn113-Pro114 peptide groups of RNase A under unfolding conditions.

155 Onconase (ONC) is a homolog of RNase A that is in clinical trials as a cancer chemother

156 ls than is any known variant or homologue of RNase A including Onconase, an amphibian homologue in ph

157 Like other mammalian homologues of RNase A, ANG forms a femtomolar complex with the cytosol

158 icate identical extents of immobilization of RNase A via the two schemes.

159 409, was sufficient to abolish inhibition of RNase A and human pancreatic RNase.

160 Thus, OVS is both a useful inhibitor of RNase A and a potential bane to chemists and biochemists

161 d (OVS) are shown to be potent inhibitors of RNase A that exploit these interactions.

162 ng-lived disulfide-insecure intermediates of RNase A, and oxidize them directly under stable conditio

163 Analysis of folding kinetics of RNase A and other proteins reveals that the highly evolv

164 ese features are discussed using kinetics of RNase A.

165 cells, and the resulting different levels of RNase A-NBC reactivation, RNase A-NBC shows a significan

166 model the transition state and mechanism of RNase A.

167 n-permeabilized oocytes or microinjection of RNase A into the oocyte released essentially all of the

168 r to what is observed for the H48A mutant of RNase A and in contrast to WT enzyme.

169 The reduction of the P93A mutant of RNase A proceeds through a single intermediate, the des

170 72S], a three-disulfide-containing mutant of RNase A which regenerates from its two-disulfide precurs

171 er, the construction of a septuple mutant of RNase A, retaining a single cysteine residue, demonstrat

172 lding events in single-tryptophan mutants of RNase A were investigated by fluorescence measurements b

173 involved in the oxidative folding pathway of RNase A, was destabilized.

174 he overall conformational folding pathway of RNase A.

175 de bonds on the oxidative folding pathway of RNase A; it also facilitated the isolation of des [58-11

176 tes, and the oxidative folding processes, of RNase A.

177 romatic thiols increased the folding rate of RNase A by a factor of 10-23 over that observed for glut

178 The hinge region of RNase A contains a proline at residue 114 that adopts a

179 Stepwise selection of RNase A and metal binding produced a dual-specific antib

180 ions representing the free energy surface of RNase A using chemical shifts as replica-averaged restra

181 ivity of GST-vhs as being similar to that of RNase A.

182 ic activity, which is far lower than that of RNase A.

183 approximately 10(4)-fold slower than that of RNase A.

184 h a catalytic efficiency approaching that of RNase A.

185 tween 1.7 and 1.3 times faster than those of RNase A at the temperatures that were investigated.

186 B were determined to be similar to those of RNase A in that two structured intermediates, each lacki

187 ntermediates of RNase B compared to those of RNase A.

188 However, the treatment of RNase A-NBC with hydrogen peroxide (one major intracellu

189 t with the known macroscopic pK(a) values of RNase A.

190 Amphibian homologues and variants of RNase A that evade RI are cytotoxic.

191 "knobs" and "holes", we designed variants of RNase A that evade RI.

192 This and two related variants of RNase A were more toxic to human cancer cells than was O

193 erize complexes of RI with a wide variety of RNase A variants and homologues, including those with cy

194 wo site-directed mutants (Y92F and Y115F) of RNase A.

195 Limited proteolysis of RNase-A yields a short N-terminal S-peptide segment and

196 kb on chromosome 6, the coding sequences of RNases A-1 and A-2 are diverging under positive selectio

197 Despite voluminous research on RNase A, the importance of many residues identified here

198 together, hydrogen exchange (HX) studies on RNase A at pH* 6.35 were used to investigate the basic t

199 Unlike ONC, RNase A contains a KFERQ sequence (residues 7-11), which

200 , recombinant angiogenin, but not RNase 4 or RNase A, induces tiRNA production and inhibits protein s

201 oriented RNase A over the randomly oriented RNase A was also apparent in the orientational behavior

202 The higher binding ability of the oriented RNase A over the randomly oriented RNase A was also appa

203 adopts the same fold as angiogenin and other RNase A paralogs, but the toxin does not share sequence

204 The RNase 8 gene is linked to seven other RNase A superfamily genes on chromosome 14.

205 mmobilized with a preferred orientation over RNase A immobilized with a random orientation.

206 Scrambled RNase A is fully oxidized RNase A with a relatively random distribution of disulfi

207 iogenin, encoding a member of the pancreatic RNase A superfamily, segregate with ALS.

208 titution increased the K(d) value of the pRI.RNase A complex by 20 x 10(6)-fold (to 1.4 microM) with

209 mple a reaction system involving the protein RNase A, its inhibitor CMP, the osmolyte urea, and water

210 compare the unfolding profiles of a protein (RNase A) and a glycoprotein (RNase B) as measured by Ram

211 of macromolecular damage, effecting protein (RNase A) photocross-linking and peptide (melittin) photo

212 cal approach to reversibly modulate protein (RNase A) function and develop a protein that is responsi

213 ed RNase L, viral RNAs cleaved with purified RNase A and RNA from uninfected and poliovirus-infected

214 to other ribosome-release agents: puromycin, RNase A/EDTA, and sodium hydroxide.

215 red protein, fully reduced ribonuclease A (r-RNase A), have been measured using synchrotron-based sma

216 ifferent levels of RNase A-NBC reactivation, RNase A-NBC shows a significant specific cytotoxicity ag

217 ium conformational ensemble of fully reduced RNase A resembles the transient conformational ensemble

218 state; rather, it is suggested that reduced RNase A has a little bias toward a native topology.

219 volution and function of two closely related RNase A ribonucleases from the chicken, Gallus gallus.

220 nt a detailed study of functionally relevant RNase A dynamics in the wild type and a D121A mutant for

221 are replicated; the correspondence to the RI-RNase A complex is somewhat greater, but still modest.

222 I is one of the strongest known, with the RI.RNase A complex having a K(d) value in the femtomolar ra

223 regions in the molecular interface of the RI.RNase A complex that exhibit a high degree of geometric

224 the genes of bovine pancreatic ribonuclease (RNase A) and human angiogenin, and a genetic selection b

225 a homolog of bovine pancreatic ribonuclease (RNase A) from the frog Rana pipiens.

226 mbers of the bovine pancreatic ribonuclease (RNase A) superfamily with an affinity in the femtomolar

227 homologue of bovine pancreatic ribonuclease (RNase A) that induces neovascularization.

228 del protein, bovine pancreatic ribonuclease (RNase A), decreases upon binding to its cognate inhibito

229 homologue of bovine pancreatic ribonuclease (RNase A).

230 inhibitor of bovine pancreatic ribonuclease (RNase A).

231 r catalysis of RNA cleavage by ribonuclease (RNase) A can exceed 10(9) M(-1) s(-1) in a solution of l

232 e concentrations of the native ribonuclease (RNase) A protein and RNase B glycoprotein within mixture

233 Members of the ribonuclease (RNase) A superfamily participate in a diverse array of b

234 les (keratin 25, trichohyalin, ribonuclease, RNase A family, 7) and inflammation-related molecules (S

235 Scrambled RNase A is fully oxidized RNase A with a relatively rand

236 s of 1, the folding of reduced and scrambled RNase A at pH 7.0 and 7.7 in the presence of 1 and gluta

237 ty to increase the folding rate of scrambled RNase A.

238 th documented data obtained by the scrambled RNase-A-based assay.

239 appeared required for this retention, since RNase A treatment of Triton-permeabilized oocytes or mic

240 bout whether chloride binds to or stabilizes RNase A.

241 cts with chaperone Hsc70 and a CMA substrate RNase A with comparable affinity but not with Hsp40 and

242 Taken together the data imply that RNase A is in a preexisting dynamic equilibrium between

243 These observations suggest that RNase A-like toxins are commonly deployed in inter-bacte

244 The RNase A superfamily has been important in biochemical, s

245 ase 4 and RNase 5/ang 1 are unique among the RNase A ribonuclease genes in that they maintain a compl

246 ithout the tertiary structure imposed by the RNase A backbone.

247 is similar to the activation barrier for the RNase A catalyzed reaction and thus would not be thermod

248 The measured Kd values for the RNase A-CMP and Cel6A D117Acd-G3 complexes were found to

249 enzyme in which a 6-residue loop 1 from the RNase A homologue, eosinophil cationic protein (ECP), re

250 the mechanism of millisecond motions in the RNase A catalytic cycle.

251 namically and functionally reproduced in the RNase A scaffold upon creation of a chimeric hybrid betw

252 avorable Coulombic interactions occur in the RNase A.OVS complex.

253 andard with the target and employment of the RNase A digestion step allow accurate and reproducible q

254 one cleavage-transesterification step of the RNase A enzyme remains controversial even after 60 years

255 otherwise canonical among the members of the RNase A gene superfamily.

256 icate a 4-fold higher binding ability of the RNase A immobilized with a preferred orientation over RN

257 erspective on the molecular evolution of the RNase A superfamily, as well as an impetus for applying

258 giogenin (hANG), an angiogenic member of the RNase A superfamily, have been recently reported in pati

259 (ANG), a 14.2-kDa polypeptide member of the RNase A superfamily, is an angiogenic protein that has b

260 The crystal structure of the RNase A/pTppAp complex was determined and demonstrates t

261 non-vertebrate protein found to possess the RNase A superfamily fold, and homologs of this toxin are

262 cleaves the NBC conjugation and restores the RNase A activity.

263 This and other evidence suggests that the RNase A superfamily originated from an RNase 5-like gene

264 average of 1640 s(-1) and is similar to the RNase A k(cat) value of 1900 s(-1).

265 rived neurotoxin (EDN), which belongs to the RNase A superfamily.

266 Thus, RNase A has evolved to become an enzyme limited by physi

267 Thus, RNase A-NBC can be reactivated inside tumor cells by hig

268 When applied to RNase A, the method revealed little or no bias toward fo

269 binding of the product analogue, 3'-CMP, to RNase A(ECP) results in only minor chemical shift change

270 Compared to RNase A, ONC utilizes more efficient interactions along

271 g to ribonuclease A (RNase A) contributes to RNase A folding and stability.

272 HIV-1 capsids were almost as insensitive to RNase A as GagZip capsids, suggesting that RNA is not a

273 formed by GagZip proteins are insensitive to RNase A, as expected.

274 rimetric data show that binding of pTppAp to RNase A is exothermic (DeltaH = -60.1 +/- 4.1 kJ/mol) wi

275 f the ribonuclease inhibitor protein (RI) to RNase A on these surfaces was characterized by using ell

276 e analogues bind more tightly to ANG than to RNase A, and are the first small molecules shown to exhi

277 hibitor protein (RI), which binds tightly to RNase A and monomeric BS-RNase.

278 uction of RI diminishes the potency of toxic RNase A variants, but has no effect on the cytotoxicity

279 stark contrast to dimerization of wild-type RNase A, which requires incubation under extreme conditi

280 ational propensities of reductively unfolded RNase A under folding conditions, since earlier work has

281 Unlike RNase A, BS-RNase has notable toxicity for human tumor c

282 activity inhibiting RNase L or the unrelated RNases A and T1.

283 Using RNase A as a model enzyme system, we show that crystals

284 Using RNase A as a model system, we validate our fibrillogenic

285 ata are consistent with a mechanism in which RNase A associates with RNA in an intermediate complex,

286 As with RNase A and beta-lactoglobulin, beta1 exhibits variable

287 me range access, (iii) biocompatibility with RNase A, and (iv) explicit treatment of mixing for impro

288 d to the several hundred-fold decreases with RNase A and Ang, and individual mutations of three other

289 np(0/0) (PrP knockout) brain homogenate with RNase A or micrococcal nuclease inhibited hamster but no

290 strate binding sites in its interaction with RNase A.

291 s abolished by the incubation of nuclei with RNase A or DNase, indicating that the interaction depend

292 Previous studies on the complexes of RI with RNase A and angiogenin revealed that RI utilises largely

293 f the bps signal, extracts were treated with RNase A, Proteinase K, or heat.

294 NMR backbone chemical shifts compared to WT RNase A.

295 Previous oxidative folding results for wt-RNase A indicated the predominance of the des [40-95] in

296 ll with the corresponding distribution in wt-RNase A and with distributions based on calculations of

297 pulation of the [65-72] disulfide bond in wt-RNase A, these results indicate a critical role for the

298 iates of [C65S, C72S] compared to that of wt-RNase A lends support for a physicochemical basis for th

299 72] disulfide bond in the regeneration of wt-RNase A.

300 compared to its analogue (des [65-72]) of wt-RNase A.