ライフサイエンスコーパス: folding rate

1 es primarily with unfolding rate rather than folding rate.

2 folding rates at the temperature of maximum folding rate.

3 in the turn or loop region mostly affect the folding rate.

4 pared it with the corresponding experimental folding rate.

5 of peptide backbone, thereby increasing the folding rate.

6 p leading to significant enhancements in the folding rate.

7 which sets the maximum possible (two-state) folding rate.

8 ation results in a 5-fold retardation of the folding rate.

9 ntly more stable, showing a 100 times faster folding rate.

10 ically decreased stability but increased the folding rate.

11 ive position, thereby decreasing the overall folding rate.

12 pendent experimental method to determine the folding rate.

13 itions under which frustration increases the folding rate.

14 d a web of nonnative states slow the average folding rate.

15 environment influences protein stability and folding rate.

16 to quantify the influence of knotting on its folding rate.

17 tural rearrangements that control the global folding rate.

18 Macroscopically, this results in faster folding rates.

19 e them from kinetic traps and increase their folding rates.

20 otein in the cis cavity, produces effects on folding rates.

21 t sequences with longer loops display slower folding rates.

22 apparent equilibrium constants and relative folding rates.

23 ir complex topologies and intrinsically slow folding rates.

24 erived from known structures correlates with folding rates.

25 f native state contact orders for predicting folding rates.

26 uffer unfolding are similar, as are in vitro folding rates.

27 ry different temperature dependencies of the folding rates.

28 teins gives rise to their topology-dependent folding rates.

29 and obtained coefficients that predict their folding rates.

30 ter describe the role of topology in protein-folding rates.

31 o be the most important determinant of their folding rates.

32 n misfolded conformations, and non-Arrhenius folding rates.

33 gnificant correlation with the logarithms of folding rates.

34 walls induces a very strong reduction of the folding rates.

35 s that cover a wide range of stabilities and folding rates.

36 of the mechanism by which urea enhances RNA folding rates.

37 Indeed, both the raw TIP3P folding rate (4.5 +/- 2.5 micros) and the diffusion-cons

38 Although the folding rate accelerates as the viscosity declines, it t

39 d the relationship between RNA structure and folding rates accounting for hierarchical structural for

40 itive correlation between hydrophobicity and folding rate across all of the residues we have characte

41 The resulting (un)folding rates agree well with experiments.

42 d TZ1 and TZ2 properties well; the estimated folding rates agreed with the experimentally determined

43 The folding rate also appeared to be influenced by differenc

44 Moreover, we find that the logarithm of the folding rates also scale as R(-gamma(c)), with deviation

45 llent agreement with experimentally measured folding rates, although pathways sampled in these simula

46 play an important role in dictating relative folding rates among topologically equivalent proteins.

47 erent members, with a 5000-fold variation in folding rate and 3000-fold variation in unfolding rate s

48 tution indicate a strong correlation between folding rate and charge state.

49 export competence is related to the protein folding rate and could be exploited for the isolation of

50 a linear relationship between the log of the folding rate and DeltaG* (H2O) .

51 tein plays a primary role in determining the folding rate and mechanism of relatively small single-do

52 ng linear correlation between the log of the folding rate and stability for this set of proteins.

53 sidues 509-511 and only minor differences in folding rate and stability.

54 mate is based on the correlation between the folding rate and the number of predicted long-range cont

55 To increase the folding rate and to gain insight into the folding proces

56 DCOMPLEX & DDNA); TCD, a program for protein-folding rate and transition-state analysis of small glob

57 for the role of unfolded chain diffusion on folding rates and barrier heights are discussed.

58 e toward the folded state by both increasing folding rates and decreasing unfolding rates.

59 ic core but that are predicted to affect the folding rates and dynamics dramatically.

60 To determine the extent to which protein folding rates and free energy landscapes have been shape

61 the concentration dependence of the observed folding rates and intermolecular FRET measurements.

62 test of such models, provide predictions of folding rates and mechanisms for a comprehensive set of

63 The prediction of protein folding rates and mechanisms is currently of great inter

64 predict the effects of mutations on protein folding rates and mechanisms would greatly facilitate fo

65 explanation for the experimentally measured folding rates and mechanisms, in terms of the intrinsic

66 es agreed with the experimentally determined folding rates and native conformations were the global p

67 logy plays a key role in determining protein-folding rates and pathways.

68 imulation, to study protein kinetics through folding rates and population kinetics from approximate f

69 Upon tethering, we find that folding rates and stability are impacted differently by

70 ure, there is no simple relationship between folding rates and stability for the archael histones.

71 disulfide bridges: large variability in both folding rates and stability of intermediates, multi-stat

72 sms by comparing the effects of mutations on folding rates and stability, but determining varphi-valu

73 of polyglutamine guest inserts, the kinetic folding rates and structural perturbation of these CI2 i

74 can be used to extract population kinetics, folding rates and the formation of particular substructu

75 Plotting the folding rates and the reduced contact order from ten dif

76 or diffusive barrier crossing, including the folding rates and the transition time for crossing the b

77 tic interactions have a pronounced effect on folding rates and thermodynamic stability.

78 protein conformational dynamics, but protein folding rates and transition times have not been calcula

79 an drastically change the protein stability, folding rate, and cooperativity.

80 his stability increase greatly increases the folding rate, and suggests that the transition state ens

81 uorescence and CD experiments yield the same folding rate, and the chevron plots have the characteris

82 m expressed in terms of transcription speed, folding rates, and metabolite binding rates predicts dif

83 The diverse folding rates appear to reflect large differences in the

84 The folding rate approaches the diffusion-limited value and

85 m the data agrees well with the experimental folding rate (approximately 640/s).

86 The equilibrium stability and the folding rate are found to be strongly dependent upon the

87 Further, these predicted folding rates are correlated strongly with contact order

88 The folding rates are faster for designed variants compared

89 In the presence of a crowding agent, folding rates are faster in the two-state regime, and at

90 The observed folding rates are found to be proportional to the number

91 Much lower folding rates are predicted when the folding is initiate

92 uch proteins frequently are hindered because folding rates are too fast to measure using conventional

93 We show that observed folding rates are well predicted by a Kramers model with

94 Errors in the folding rates arising from instrument artifacts were onl

95 efolding rate in the 193 region and a faster folding rate around the active site (86, 41, 73 regions)

96 The folding rate at 300 K is (0.7 micros)(-1) with little or

97 Remarkably, the calculated folding rate at [C] = 0 is only 16-fold larger than the

98 o-Hyp)(4) region significantly decreases the folding rate at low but not high concentrations, consist

99 e sequences used exhibit a 600-fold range of folding rates at the temperature of maximum folding rate

100 on found between experimental and calculated folding rates based on free energy barrier heights using

101 compact denatured polypeptide can limit the folding rate, but the limiting time scale is very fast.

102 e same region of a beta-strand decreased the folding rate by 20- and 50-fold, respectively, suggestin

103 inhibitor 2 (CI2), accelerates the protein's folding rate by a factor of 36 relative to that of the w

104 anine residue with alanine will increase the folding rate by removing a transient non-native interact

105 ng Asp46 with Ala leads to a decrease in the folding rate by roughly 9 times.

106 ntramolecular interactions influence protein folding rates by altering dynamics and not activation fr

107 t rather adopts an active role, accelerating folding rates by decreasing the roughness of the energy

108 hain models of natural proteins with diverse folding rates by extensive comparisons between the distr

109 majority (55%) of these substitutions affect folding rates by less than a factor of 2, and that only

110 than a factor of 2, and that only 9% affect folding rates by more than a factor of 8.

111 a protein and provide insights into how its folding rate can be modified during evolution by mutatio

112 erstand the molecular basis of the decreased folding rate, changes in the unfolded as well as the fol

113 ment between simulation and experimental CI2 folding rates, CI2 structural perturbation, and polyglut

114 me in the unfolded state (the inverse of the folding rate coefficient).

115 the unfolded protein is extremely large, the folding rate coefficient, k(f), is much smaller than k(a

116 Whereas the folding rate coefficients differ by a factor of 10,000,

117 onds within the turn region elicits a slower folding rate, consistent with the hypothesis that these

118 , the corresponding estimated values for the folding rate constant are larger by two to three orders

119 Rs, a second exponential phase with a slower folding rate constant is observed.

120 The 1.9-fold increase in folding rate constant observed for this change at the ch

121 pient downhill folder having an extrapolated folding rate constant of 2 x 10(5) s(-1) and a stability

122 ve similar unfolding rate constants, but the folding rate constant of gcUUCGgc is 4.1-fold faster at

123 erature dependence of the natural log of the folding rate constant suggests that folding occurs via a

124 of slope in the plot of the logarithm of the folding rate constant versus denaturant concentration, c

125 ease is largely correlated with an increased folding rate constant, and with a smaller but significan

126 The folding rate constants approached limiting values with i

127 te state is significantly populated, and the folding rate constants are relatively slow compared to t

128 cal peptides and from demonstration that the folding rate constants for coiled coils, as obtained by

129 The extrapolated folding rate constants in water at 298 K were 210,000 s(

130 With increasing calcium, the folding rate constants increase while unfolding rate con

131 mula fits well the experimentally determined folding rate constants of the 24 proteins, with single v

132 Experiments have shown that the folding rate constants of two dozen structurally unrelat

133 erted together into R16 or R17, increase the folding rate constants, reduce landscape roughness, and

134 families, stability is also a determinant of folding rate constants.

135 In contrast, the folding-rate constants are almost identical for the thre

136 When compared at an isostability point, the folding rates converged to a similar value and there is

137 -folding field is whether unfolding rates or folding rates correlate to the stability of a protein.

138 The accelerated folding rates could result from helix stabilization with

139 Under most conditions, the observed folding rate decreases with increasing counterion concen

140 folding can either speed up or slow down the folding rate depending on the amount of native and nonna

141 her accelerated or retarded compared to bulk folding rates, depending on the temperature of the simul

142 We find that the logarithm of the folding rate depends linearly on the entropic change ass

143 eely jointed chain models illustrate how the folding rate depends on the entropic and enthalpic energ

144 The folding rate determined for these cyclic peptides is acc

145 lusion of beta-turn mimics alters beta-sheet folding rates, enabling us to classify beta-turn mimics

146 In addition the 5-6-fold folding rate enhancement varied only slightly with pH, 7

147 In all cases examined, the folding rate enhancement with the aromatic thiol was 5-

148 These substrate proteins experience folding rate enhancements without undergoing multiple ro

149 The folding rates extracted using a simple kinetic model are

150 bility, and that the experimentally measured folding rates fall within this narrow triangle built wit

151 e slow diffusion that markedly decreases the folding rate for a designed alpha-helical protein.

152 results showing, if anything, a slowdown in folding rate for encapsulated Rhodanese.

153 had a nonnative free-energy minimum, and the folding rate for OPLS(aa) TZ3 was sensitive to the initi

154 is well-correlated with the logarithm of the folding rate for these small, well-characterized molecul

155 ness holds over a surprisingly wide range of folding rates for our designed sequences.

156 den triangle" limiting the possible range of folding rates for single-domain globular proteins of var

157 t with experimentally derived structures and folding rates for specific systems, leaving them positio

158 The folding rates for telomeric RNA and DNA G-quadruplexes a

159 thermodynamic and kinetic quantities such as folding rates, free energies, folding enthalpies, heat c

160 Here, we estimate two-state folding rates from predictions of internal residue-resid

161 dary structure prediction methods to predict folding rates from sequence alone.

162 dary structure had been exploited to predict folding rates from sequence.

163 ally, Kramers theory was used to predict the folding rates from the landscape profile, recovering the

164 t of many experimental studies, but its slow folding rate has made it difficult to observe and charac

165 tabilization of I(2)* correlated with slower folding rates, implying that NNS is not a kinetic trap b

166 ightly steeper temperature dependence of the folding rate in some cells that can be rationalized in t

167 The folding rate in the absence of denaturant is 260 s(-)(1)

168 We find that enhancement of the folding rate in the second, rate-limiting step is correl

169 between experimental observed and predicted folding rates in jackknife cross validation.

170 to contribute to the viscosity dependence of folding rates in larger proteins.

171 trapolating GuHCl-based chevrons to estimate folding rates in the absence of denaturant and in interp

172 The folding rates in the absence of denaturant were found to

173 thiol was initially determined and then the folding rates in the presence of each thiol were measure

174 The trends in folding rates in the presence/absence of gatekeepers obs

175 The folding rate increases due to reduced-dimension pathways

176 5.0 to 6.40 kcal mol(-1) at pH 8.0 while the folding rate increases from 0.60 to 18.7 s(-1).

177 Analysis of the urea dependence of the folding rates indicates that mutations modulate the unfo

178 /B/G/H helix core substantially decrease the folding rate, indicating that docking and folding of the

179 The folding rate is 640 s(-1) and the value of deltaG degree

180 The net folding rate is a product of the equilibrium constant of

181 as the sole factor to determine the hairpin-folding rate is an oversimplification.

182 At a higher force (f = 11 pN), the folding rate is controlled by the formation of the bulge

183 What controls the folding rate is hotly debated.

184 The folding rate is not retarded by populating an intermedia

185 ions), the influence of these factors on the folding rate is poorly understood.

186 rotein folds in a two-state fashion, and the folding rate is slow.

187 es that the topology-dependence of two-state folding rates is a direct consequence of the extraordina

188 racy of total contact distance in predicting folding rates is essentially unchanged if "short"-ranged

189 ethanol cosolvent allows us to determine the folding rate (kf approximately 0.3 (micros)(-1)) and the

190 en able to predict the temperature-dependent folding rate, kinetic intermediates, and folding pathway

191 r the observation of "chevron behavior" (log folding rate linear in denaturant concentration) typical

192 phobicity of a side-chain and the log of the folding rate, ln(k(f)).

193 ar relationship between stability (logK) and folding rates (logk(f)) over the range of pH 5-9 for all

194 Moreover, starting structures with folding rates most similar to experiment show some nativ

195 Accordingly, the folding rate must be slower than the product of the frac

196 in folding does not speed up the polypeptide-folding rate; nevertheless, it results in much faster (>

197 agree with the extrapolated barrier-limited folding rate observed near the melting transition.

198 Little change in folding rates occurred for the Ala/Gly pair mutations at

199 free energy barrier and results in a maximum folding rate of (2.0 +/- 0.3 micros)(-1), which is appro

200 The known folding rate of 20 s-1 at 1.5 M guanidinium chloride in

201 The folding rate of 26.4 mus(-1) (at 80 degrees C), extracte

202 We measure the stability and folding rate of a mutant of the enzyme phosphoglycerate

203 e studied the effect of Gly mutations on the folding rate of barnase to investigate the secondary str

204 l limiting law, both the stability and (log) folding rate of FynSH3 increase nearly perfectly linearl

205 to "zipper up," while having an extrapolated folding rate of k(f) = 2 x 10(5) s(-1).

206 We interpret the acceleration of the folding rate of MrH3a in 8% HFIP as a direct consequence

207 While GroELS increases the folding rate of PepQ by over 15-fold, we demonstrate tha

208 the effect of crowding on the stability and folding rate of protein tertiary structures, very little

209 At pH 6.0, the aromatic thiols increased the folding rate of RNase A by a factor of 10-23 over that o

210 vestigated for their ability to increase the folding rate of scrambled RNase A.

211 The folding rate of the CLN025 beta-hairpin is unchanged wit

212 0)PC liposomes resulted in a decrease in the folding rate of the fast pathway.

213 of the 5' end to G303 in J8/7 decreased the folding rate of the P4-P6 domain.

214 ding leads to an appreciable decrease in the folding rate of the shortest beta-hairpin peptide, indic

215 ore a target for engineering to increase the folding rate of the subdomain from approximately 0.5 mic

216 Folding rate of this class of proteins is positively cor

217 mical basis for the previously observed slow folding rate of this mutant, compared to its analogue (d

218 Our results suggest that the folding rate of two-state proteins is a function of thei

219 the basis of our simulations we estimate the folding rate of villin to be approximately 5micros.

220 These results contrast with folding rates of 2-0.2 s(-1) previously observed for for

221 eters, we obtain a good correlation with the folding rates of 24 two-state folding proteins.

222 ing, two-state proteins and confirm that the folding rates of a diverse set of Go 27-mers are poorly

223 igated the effects of point mutations on the folding rates of a small single domain protein.

224 lts suggest that the differences in regional folding rates of AKe are not derived from the specific d

225 The folding rates of all the other constructs were lower tha

226 To examine this division, folding rates of circularly permutated isomers are compa

227 By comparing folding rates of consensus ankyrin repeat proteins (CARP

228 imited by rates of protein synthesis, by the folding rates of its slowest proteins, and--for large ce

229 trast, SurA showed no effect on the observed folding rates of PagP, consistent with the view that the

230 We also assayed folding rates of PGK-FRET in spatial proximity to and fa

231 This model gives estimates of folding rates of proteomes, leading to a median folding

232 The oxidative folding rates of RNase B are between 1.7 and 1.3 times f

233 cused on elucidating the factors that govern folding rates of simple proteins.

234 The relative folding rates of simple, single-domain proteins, protein

235 Folding rates of small single-domain proteins that fold

236 In contrast, the relative folding rates of small, Go-potential lattice polymers, w

237 rotected in the bulk and (b) by accelerating folding rates of the protein.

238 The folding rates of the redesigned proteins are greater tha

239 The folding rates of the slow kinetics phase calculated over

240 ed by results from an Eyring analysis of the folding rates of the two proteins.

241 lation between sigma and either the relative folding rates of these proteins or the presence or absen

242 Folding rates of two-state folding proteins correlate we

243 The folding rates of two-state single-domain proteins are ge

244 with the 9 order of magnitude dependence of folding rates on protein size for a set of 93 proteins,

245 rimentally identified from the dependence of folding rates on solvent viscosity.

246 he alanine substitution has no effect on the folding rate or on the equilibrium constant.

247 misfolding is not determined by the relative folding rates or barrier heights for forming the domains

248 The nucleus increases PGK stability and folding rate over the cytoplasm and ER, even though the

249 In the example studied here, the analysis of folding rates, Phi-values, and folding pathways provides

250 The increased stability and high folding rate predicted by our simulations were subsequen

251 The posterior distribution of the folding rate predicted from the data agrees well with th

252 contact map prediction is useful for protein folding rate prediction, model selection and 3D structur

253 The model gives reliable folding rate predictions provided excluded volume terms

254 elix (helix I) unfolded, fold with identical folding rates, providing direct evidence for the conclus

255 gregation, or an active role in accelerating folding rates, remains a matter of debate.

256 d aggregation but did not alter the observed folding rates, resulting in a higher overall yield of ac

257 the protein by 1 kcal/mol and increases the folding rate sixfold, as measured by nanosecond laser T-

258 the effects of single-point mutations on the folding rate, stability, and transition-state structures

259 e of barnase do not significantly affect the folding rate, suggesting a lack of specific favorable in

260 y next to the beta-turn, does not change the folding rate, suggesting that most native interstrand H-

261 tion is completely reflected in an increased folding rate suggests that this region of the protein is

262 known correlation between contact order and folding rates, suggests that other proteins will have a

263 temperature at which it exhibits its fastest folding rate (T(m)<T(f)).

264 ilizing the hinge regions leads to twice the folding rate that is obtained from hyperstabilizing the

265 ins exhibit two-state folding kinetics, with folding rates that span more than six orders of magnitud

266 n thus does not appear to operate on protein folding rates, the majority of the designed proteins unf

267 gle, experimentally determined structure and folding rate, this does not ensure that a given simulati

268 r map-based kinetics techniques by comparing folding rates to known experimental results.

269 For confinement to positively impact folding rates under physiological conditions, it is henc

270 2.1 Single-domain chains: fast folding rates; unstable intermediates; two-state kinetic

271 presence of the salts markedly increased the folding rates (up to 5-fold).

272 transition state identified by the change in folding rate upon addition of metal ions.

273 protein exhibited a twofold acceleration in folding rates upon encapsulation.

274 The folding rate varies remarkably between different members

275 cillus subtilis RNase P RNA isomers, whereas folding rates vary by only 1.2-fold for circularly permu

276 Folding rates vary by tenfold for circularly permuted Ba

277 For a fixed pore size, the folding rates vary non-monotonically as lambda is varied

278 The ultrafast folding rate, very accurate X-ray structure, and small s

279 ding for all of the constructs; however, the folding rate was affected by their amino acid sequences

280 haracteristics of the native enzyme, but its folding rate was altered.

281 In contrast, a significant difference in folding rates was observed for the Ala/Gly pair mutation

282 hose substitutions that significantly affect folding rates, we find that accelerating substitutions a

283 Furthermore, under similar conditions folding rates were almost identical with either reduced

284 Both the opening and folding rates were found to vary with changing salt cond

285 Oxidative folding rates were further increased in the presence of

286 Two distinct folding rates were observed across a range of Mg(2+) con

287 Folding rates were observed to be either accelerated or

288 We found that the folding rates were relatively similar, approximately 0.1

289 We find a substantial acceleration of the folding rate when the connecting loop is made shorter (i

290 cs also provide a novel method for measuring folding rates when the exchange between folded and unfol

291 f a beta-hairpin primarily by increasing its folding rate, whereas a stronger hydrophobic cluster inc

292 f a beta-hairpin primarily by increasing its folding rate, whereas a stronger hydrophobic cluster inc

293 The increase in folding rate with chain length, as opposed to a decrease

294 ects of folding such as the variation of the folding rate with stability or solvent viscosity and the

295 roteins (CARPs), we find a clear increase in folding rates with increasing size and repeat number, al

296 p mutants show unusually strong increases in folding rates with marginal effects on stability.

297 ack disulfide bridges, and (ii) display slow folding rates with multi-state kinetics, to determine re

298 n path time is remarkably insensitive to the folding rate, with only a 2-fold difference for rate coe

299 by a 35-fold increase in tetraloop-receptor folding rate, with only a modest decrease in the corresp

300 ass, comprising all other residues, produces folding rates within a factor of two of the wild-type ra

301 o other hydrophobic residues often increases folding rates without significantly altering folding fre