ライフサイエンスコーパス: Gibbs free energy

1 are enthalpies, and those in parentheses are Gibbs free energies).

2 sistent with the curvature dependence of the Gibbs free energy.

3 and is the primary driving component of the Gibbs free energy.

4 spontaneous at both pH levels, with negative Gibbs free energy.

5 semblies reside at the global minimum of the Gibbs free energy.

6 he underlying cause was a positive change in Gibbs free energy.

7 well as the changes of entropy, enthalpy and Gibbs free energy.

8 conformation changes that contribute to the Gibbs free energy.

9 e conditions is examined by evaluating their Gibbs free energies.

10 Relative Gibbs free energies (133 K) calculated using B3LYP and M

11 n states, but on the basis of the calculated Gibbs free energy a +II/+IV mechanism can be excluded.

12 The remaining deviations in the Gibbs free energy (about 1 kJ/mol) are significantly sma

13 In the second tier, Gibbs free energies and corresponding free energy barrie

14 robes and on-targets or off-targets based on Gibbs free energies and melting temperatures.

15 io computational method that can predict the Gibbs free energies and thus phase diagrams of molecular

16 crobial biomass (theoretical yield) based on Gibbs free energy and microbially available electrons.

17 Using ab initio simulations, we computed Gibbs free energy and phase diagram for liquid and solid

18 ducts and used these data to calculate their Gibbs free energy and redox potential.

19 Electronic coupling matrix elements, Gibbs free energy, and reorganization energy were calcul

20 the hypernetted chain approximation for the Gibbs free energy, and we find results that are consiste

21 nductivity, carrier mobility, and a suitable Gibbs free energy are important criteria that determine

22 indicate that entropic contributions to the Gibbs free energy are important determinants of the Bolt

23 enthalpic and entropic contributions to the Gibbs free energy are important for an accurate determin

24 We also calculated Gibbs free energy as in the order of -30 kJ/mol and DHFR

25 20 degrees C reveal that, despite comparable Gibbs free energies, association with the major groove i

26 ch-containing duplexes have almost identical Gibbs free energy at 37 degrees C, with values approxima

27 perature dependence (more negative change in Gibbs free energy at increased temperature) is in agreem

28 user to batch extract the universal quantity Gibbs free energy at residue levels over multiple protei

29 e activation energy, activation entropy, and Gibbs' free energy at 50.0 degrees C were 156 kJ mol(-1)

30 ction process the highest energy barrier and Gibbs free energy barrier are all associated with the fi

31 the gas-phase NHC-CO2 bond distance and the Gibbs free energy barrier for decarboxylation is demonst

32 active complex is rate-determining and has a Gibbs free energy barrier higher than that for the first

33 Also affected were the Gibbs free energy barriers for the ring-flip and the N-i

34 tallographic structure of PixD, coupled with Gibbs free energy calculation between interacting faces

35 ivities for hydrogen evolution, according to Gibbs free energy calculations of H-adsorption on Mo2B4.

36 Gibbs free energy calculations performed on C14, C15, an

37 Using molecular dynamics simulations with Gibbs free energy calculations, we reveal that water dis

38 mitations are linked to an increased overall Gibbs free energy change (DeltaG(Overall)) and a potenti

39 transition temperature (T(m)), the unfolding Gibbs free energy change (DeltaG), and the unfolding ent

40 ckground molecules, on the estimation of the Gibbs free energy change (DeltarG) of the reactions.

41 itch determines the behavior patterns of the Gibbs free energy change and hence a change in the equil

42 rees ) showed negative entropy, enthalpy and Gibbs free energy change at 25 degrees C.

43 As cellular inputs, ketones increase Gibbs free energy change for ATP by 27% compared to gluc

44 nding on the urea concentration, and (2) the Gibbs free energy change for denaturation of Cyt c on Au

45 The Gibbs free energy change for denaturation of the protein

46 (2+), Br(-)](+*) was due to a less favorable Gibbs free energy change for electron transfer that resu

47 The Gibbs free energy change for leucine binding to the high

48 The Gibbs free energy change for leucine binding to the low-

49 f CL binding, thereby revealing the relative Gibbs free energy change for lipid binding caused by the

50 The Gibbs free energy change for reactions of inactivation o

51 of the stationary phase, is dependent on the Gibbs free energy change for these molecules at infinite

52 The results imply that the negative Gibbs free energy change minimum at a well-defined stabl

53 r at 298 K, which corresponds to a favorable Gibbs free energy change of 23 kcal/mol.

54 re smaller for rP148 than rP172, whereas the Gibbs free energy change of assembly (DeltaG(A)) was not

55 thods were utilized to estimate the standard Gibbs free energy change of every reaction in the constr

56 ssure) leads to true negative minimum in the Gibbs free energy change of reaction, deltaG(o)(T)(react

57 y as a function of temperature: the standard Gibbs free energy change, deltaG degrees, and deltaG deg

58 ons of both anesthetics result in a negative Gibbs free energy change, which in both enzymes is more

59 parent conductive oxide as a function of the Gibbs free energy change.

60 The cavitation Gibbs free-energy change (DeltaDeltaGcav = 4.78 kcal mol

61 tely resolving the intrinsic and cooperative Gibbs free energy changes describing the reactions being

62 An evaluation of Gibbs free energy changes displayed by single and combin

63 Gibbs free energy changes in diverse electrolytes exhibi

64 ip models of protein isotherm parameters and Gibbs free energy changes in ion-exchange systems were g

65 Gibbs free energy changes of reaction were calculated to

66 The difference between the binding Gibbs free energy changes of the two affinities (Delta G

67 we measured the enthalpy, heat capacity, and Gibbs free energy changes of these processes.

68 t-guest mutational strategy to calculate the Gibbs free energy changes of water-to-lipid transfer for

69 rglow oxathiine intermediates due to the low Gibbs free energy changes required for this photoreactio

70 The calculated Gibbs' free energy changes were compared with actual exp

71 doping axis, where the second derivative of Gibbs free energy (chemical susceptibility) diverges at

72 attributed to a markedly small difference in Gibbs free energy compared to the known similar class of

73 Gibbs free energy contribution values were estimated for

74 escence unfolding curves of [D]50 values and Gibbs free energy correlate well with each other and mor

75 ments would benefit from the availability of Gibbs free energy data of chlordecone and its potential

76 energy, E(a), of 42 kcal/mol, an activation Gibbs free energy, delta G(++), between 23 and 22 kcal/m

77 Gibbs free energy (DeltaG > 0), enthalpy (DeltaH > 0), a

78 The assay allows the standard Gibbs free energy (DeltaG degrees ), enthalpy (DeltaH de

79 inding constant (K = 1.10 x 10(6) M(-1)) and Gibbs free energy (DeltaG degrees = -8.26 kcal.mol(-1))

80 r predicting signal intensities by comparing Gibbs free energy (DeltaG degrees) calculations to exper

81 an that of dissociation since the activation Gibbs free energy (DeltaG(*)) was lower for the former (

82 Gibbs free energy (DeltaG(0) = -2.59 kJ mol(-1)), enthal

83 R by increasing hydrogen bonds and favorable Gibbs free energy (DeltaG) changes.

84 binding parameters revealed that the binding Gibbs free energy (DeltaG) of the new inhibitors was dom

85 thermodynamic binding parameters [changes in Gibbs free energy (DeltaG), enthalpy (DeltaH) and entrop

86 o titrate PDZ3, which yielded the changes in Gibbs free energy (DeltaG), enthalpy (DeltaH), and entro

87 T) framework to quantitatively determine the Gibbs free energy (DeltaG), enthalpy (DeltaH), and entro

88 stabilized and favored by a large change in Gibbs free energy, DeltaG degrees (-50 kJ/mol).

89 The dependence of the change in Gibbs free energy, DeltaGobs, for the diffusion of AQ th

90 tor analysis to calculate, respectively, the Gibbs free energy difference between B-DNA and P-DNA, an

91 The Gibbs free energy difference between native and unfolded

92 The generally small Gibbs free energy difference between the Z and E isomers

93 y in SrCoO(3-delta) is attributed to a small Gibbs free-energy difference between two topotatic phase

94 The alteration in Gibbs free energy encompasses contributions from both su

95 Gibbs' free energies, enthalpies, entropies, and activat

96 ectrostatic and hydrophobic contributions to Gibbs free energy, enthalpy, entropy, and heat capacity

97 to estimate thermodynamic quantities, namely Gibbs free energy, enthalpy, entropy, and heat capacity,

98 molecules are controlled specifically by the Gibbs free energy (entropy and enthalpy) of the system.

99 d free energy methods to calculate ab initio Gibbs free energies for general organic molecular materi

100 Gibbs free energies for solute transfers from gas to ret

101 rriers to the calculation and measurement of Gibbs free energies for the conversion of X to XH(n) in

102 ual steps in the model were characterized by Gibbs free energies for the equilibria and activation en

103 ope 0.8, between the activation barriers and Gibbs free energies for these TIM-catalyzed reactions.

104 c capacity (Q(max)), and hydrophilicity (the Gibbs free energy for binding water, DeltaG) as Q(max) =

105 The Gibbs free energy for converting two terminal MN(2) comp

106 with N(4)-CMdC in a 12-mer duplex increased Gibbs free energy for duplex formation at 25 degrees C b

107 x as represented by a 4 kcal/mol increase in Gibbs free energy for duplex formation at 25 degrees C.

108 olecular electron transfer in MHCF optimizes Gibbs free energy for hydrogen adsorption (DeltaG(H*) )

109 Herein, we propose the Gibbs free energy for oxygen vacancy formation in Pr(0.5

110 that these clamping side chains minimize the Gibbs free energy for substrate deprotonation, and that

111 ontains 100 mM monovalent salt, the standard Gibbs free energy for the binding of these peptides is 3

112 Association constant and Gibbs free energy for the interaction of anti-OTA/Protei

113 Association constant and Gibbs free energy for the interaction of Glass/ZnO-NRs/P

114 The Gibbs free energy for the transition to the unfolded for

115 The Gibbs free energy for this process, DeltaG(o), obtained

116 The Gibbs free energy [Formula: see text] values of NaDS + O

117 rom these surface and volume energies in the Gibbs free energy formulation.

118 eat from sources below 100 degrees C and the Gibbs free energy from salinity gradients.

119 es the affinity of each other subunit with a Gibbs free energy ( G) of ~-3.5 to ~-5.5 kJ . mol(-1), d

120 H-S4 was confirmed by both the high negative Gibbs free energy gain, DeltaG = -115.95 kJ/mol, calcula

121 C) between predicted and measured changes of Gibbs free-energy gap, DeltaDeltaG, upon mutation reache

122 The suggested requirements comprised Gibbs free energy >= -7.5 kcal mol(-1) and melting tempe

123 trifugation, which only provide affinity and Gibbs-free energy (i.e., K(D) and DeltaG), are employed.

124 ) and vWbp(1-474), with a 30-45% increase in Gibbs free energy, implicating a regulatory role for fra

125 The reaction Gibbs free energies indicate that all reactions are virt

126 ilizes computed hydrogen atom transfer (HAT) Gibbs free energy instead of E(H)(1) as a predictor was

127 stead of NAD(H) saves a greater share of the Gibbs-free energy, instead of wasting it as heat.

128 The Gibbs free energy is calculated as a function of P/L and

129 Available Gibbs free energy is reduced by 71 to 86% across the hab

130 someric transformation demonstrates that the Gibbs free energy is the driving force for the transform

131 enable the experimental determination of the Gibbs free energy landscape along the Psi reaction coord

132 rectly coupled to their local environment or Gibbs free energy landscape as defined by solvent, tempe

133 a and the Ramachandran Psi angle (un)folding Gibbs free energy landscape coordinate of a mainly polya

134 n the conformational equilibria and relative Gibbs free energy landscapes along the Ramachandran Psi-

135 At the heart lies the exploration of the Gibbs free-energy landscapes and the extended phase diag

136 hybrid material, a discrepancy occurs in the Gibbs free energy leading to a difference in oxidation p

137 al equilibrium problems are solved using the Gibbs Free Energy minimization method.

138 ontrol and that their shape is determined by Gibbs free energy minimization.

139 We find the unfolding kinetics and Gibbs free energies obtained from all three methods to b

140 The obtained Gibbs free energies of activation are in the range 7-22

141 e cyclization reactions are substantial with Gibbs free energies of activation between 19 and 40 kcal

142 and desorption can be attributed to the high Gibbs free energies of activation for forming and breaki

143 negative correlation between the calculated Gibbs free energies of activation for the modeled reacti

144 enate into monodentate surface complexes had Gibbs free energies of activation ranging from 62 to 73

145 plexes to bidentate, binuclear complexes had Gibbs free energies of activation ranging from 79 to 112

146 whereas the ab initio heats, entropies, and Gibbs free energies of adsorption are used to assess the

147 Gibbs free energies of adsorption demonstrated weak comp

148 27-Mg (Mg-MOF-74), ab initio calculations of Gibbs free energies of adsorption have been performed.

149 er supported by energy estimates in that the Gibbs free energies of binding and catalysis for the qua

150 cytolytic peptides in model membranes to the Gibbs free energies of binding and insertion into the me

151 Furthermore, the Gibbs free energies of binding and insertion of the pept

152 predicted stereoselectivities using computed Gibbs free energies of diastereomeric transition states

153 ar orbital calculations and with theoretical Gibbs free energies of hydration to describe aqueous ion

154 ors governing selectivity, we quantified the Gibbs free energies of interactions of the peptide with

155 The Gibbs free energies of oxygen transfer from these hetero

156 DFT calculations of the Gibbs free energies of possible isomers were performed t

157 Gibbs free energies of reaction depended on the net char

158 The highest Gibbs free energies of reaction for physical adsorption

159 Enthalpies and Gibbs free energies of reaction obtained from Born-Fajan

160 activation ranging from 79 to 112 kJ/mol and Gibbs free energies of reaction ranging from -11 to -55

161 e proceeded with no activation barrier, with Gibbs free energies of reaction ranging from -21 to -58

162 activation ranging from 62 to 73 kJ/mol, and Gibbs free energies of reaction ranging from -23 to -38

163 Gibbs free energies of reactions with various free radic

164 examined the relationship between calculated Gibbs free energies of the cluster formation and experim

165 The Gibbs free energies of the transition states with the na

166 Analysis of the Gibbs free energies of these two reactions guides the se

167 uctures and association constants (K(a)) and Gibbs free energies of transfer for GLY-humic complex fo

168 (Trp-7) exhibit the greatest stability, with Gibbs free energies of unfolding in the absence of denat

169 NO3(-), SO4(2-), Na(+), and NH4(+) and find Gibbs free energies of water displacement of -10.9, -22.

170 r [Al(CH(3))(2)](+) abstraction (a change in Gibbs free energy of 0.0 kilocalories per mole).

171 lytic activities correlate linearly with the Gibbs free energy of 1-butene adsorption.

172 G(d,p) level of theory, giving an activation Gibbs free energy of 11.9 kcal/mol for water environment

173 We analyze the definition of the Gibbs free energy of a nanoparticle in a reactive fluid

174 raction of GA and ChCl substantially reduced Gibbs free energy of acetal reaction and thoroughly capt

175 l1 interconversion is, however, slow, with a Gibbs free energy of activation as high as 28.5 kcal/mol

176 The related Gibbs free energy of activation has been calculated as 2

177 olysis reaction for dynamic reasons, and its Gibbs free energy of activation is 19.3 kcal/mol and rem

178 nd -64.1 J mol(-1) K(-1), respectively, with Gibbs free energy of activation ranging from 97.5 kJ mol

179 nt of 3(1) x 10(7) M(-1), corresponding to a Gibbs free energy of adsorption of -52.6(8) kJ/mol, and

180 s strongly attracted to the interface with a Gibbs free energy of adsorption of -6.8 kcal/mol.

181 monic generation spectroscopy to measure the Gibbs free energy of adsorption of both carbonate (CO(3)

182 er and a monolayer of dodecanol, wherein the Gibbs free energy of adsorption was determined to be -6.

183 tants, the surface equilibrium constant, the Gibbs free energy of adsorption, and the surface coverag

184 , we show through direct measurements of the Gibbs free energy of adsorption, combined with theory an

185 s at multiple concentrations, we extract the Gibbs free energy of adsorption, finding it larger than

186 entropic and enthalpic contributions to the Gibbs free energy of adsorption.

187 inorganic phosphate, adenosine diphosphate, Gibbs free energy of ATP hydrolysis (DeltaGATP), phospho

188 acidic pH results in a large decrease in the Gibbs free energy of binding but no change in the enthal

189 c analysis indicates that the less favorable Gibbs free energy of binding reflects a substantial enth

190 We found that the Gibbs free energy of binding to a POPC surface at low pH

191 itions from various sources to calculate the Gibbs Free Energy of biosynthesis independently of speci

192 The partial Gibbs free energy of Ca in six Ca-Pb-Sb alloys was deter

193 The modeled partial Gibbs free energy of calcium in Ca-Ag, Ca-In, Ca-Pb, Ca-

194 The partial Gibbs free energy of calcium in Ca-Bi liquid alloys at 6

195 The Gibbs free energy of dimer dissociation of HIV-1 RT is d

196 n the effect of the analyte content over the Gibbs free energy of dispersions, affecting the thermody

197 mic properties such as enthalpy, entropy and Gibbs free energy of dissolution were obtained using exp

198 s in approximately 1 kcal/mol less favorable Gibbs free energy of duplex formation at 37 degrees C.

199 e the rate of racemization and calculate the Gibbs free energy of enantiomerization (DeltaG(*)(Enant)

200 e; (2) electric-field induced differences in Gibbs free energy of exfoliation; (3) dispersion of MoS2

201 Thermodynamic calculations showed that the Gibbs free energy of Fe(II) oxidation (DeltaG(oxidation)

202 is is introduced for estimating the standard Gibbs free energy of formation (Delta(f)G'(o)) and react

203 Calculated enthalpy and Gibbs free energy of formation at 298 K for NO3- and ReO

204 between ionic potential and the enthalpy and Gibbs free energy of formation for previously measured o

205 The Gibbs free energy of formation of zinc peroxide was foun

206 The redox potential is calculated via the Gibbs free energy of formation, PCB concentrations in re

207 ueous medium is rare, owing to the very high Gibbs free energy of hydration and ambiguity to distingu

208 ude, following a trend dictated by the ions' Gibbs free energy of hydration.

209 drogenolysis selectivity correlates with the Gibbs free energy of hydrogen adsorption.

210 3) possesses a thermal neutral and desirable Gibbs free energy of hydrogen for HER, ascribed to the t

211 5 A of the phosphorylation site--encode the Gibbs free energy of inhibition (DeltaG(inhibition)) for

212 tical micellar concentration (CMC), standard Gibbs free energy of micellization (DeltaG(0)mic.) etc.

213 The Gibbs free energy of mixing dissipated when fresh river

214 and porous carbon electrodes to convert the Gibbs free energy of mixing sea and river water into ele

215 everse electrodialysis (RED) can harness the Gibbs free energy of mixing when fresh river water flows

216 w that it is less than the ideal work (i.e., Gibbs free energy of mixing) due to inefficiencies intri

217 g thermodynamic integration, we estimate the Gibbs free energy of mixing, thereby determining the tem

218 a reversible PRO process is identical to the Gibbs free energy of mixing.

219 utions of different composition releases the Gibbs free energy of mixing.

220 of total mixed solution, which is 57% of the Gibbs free energy of mixing.

221 a reversible RED process is identical to the Gibbs free energy of mixing.

222 The contribution to the Gibbs free energy of phase transfer for the passage of a

223 hibited domain organization due to favorable Gibbs free energy of phospholipid mixing.

224 This model connects the activation Gibbs free energy of point defects formation and migrati

225 he second complete accounting of the cost in Gibbs free energy of protein transport to be undertaken.

226 study function to reduce the standard-state Gibbs free energy of reaction for deprotonation of the w

227 ty and methanogenic potential than favorable Gibbs free energy of reaction.

228 l enthalpic and entropic contribution to the Gibbs free energy of retention.

229 onducting multiple linear regression between Gibbs free energy of sorption and Abraham descriptors fo

230 alorimetry (DSC) enabled a dissection of the Gibbs free energy of stability into enthalpic and entrop

231 me was found to unfold cooperatively, with a Gibbs free energy of stabilization (DeltaG(0)) of 32 +/-

232 The Gibbs free energy of surface adsorption can be accuratel

233 ical theory to compute approximations to the Gibbs free energy of the binding interaction between the

234 ifferential mobility on the reduced mass and Gibbs free energy of the cluster formation.

235 r: from Z-enol1 to E-enol1, due to the lower Gibbs free energy of the E-enol1 anion.

236 The thermodynamic Gibbs free energy of the E/Z equilibrium of the isomers

237 The changes in the Gibbs free energy of the enzyme-substrate complex (Delta

238 We experimentally determined the Gibbs free energy of the folding process (DeltaG(eq)) in

239 usters grown atop Ru exhibit a close-to-zero Gibbs free energy of the hydrogen adsorption, promoting

240 The electrostatic potential and the Gibbs free energy of the self-assembled materials were u

241 estimate the enthalpy, the entropy, and the Gibbs free energy of the surfactant/analyte complexes.

242 of Rh carbene into water are due to the low Gibbs free energy of the transition state for the concer

243 The Gibbs free energy of this process (DeltaG0) is approxima

244 Although the magnitude of the incremental Gibbs free energy of transfer for a methylene segment is

245 omparing values of nonpolar surface area and Gibbs free energy of transfer for the different amino ac

246 Finally, we evaluate the Gibbs free energy of transfer of individual lipid compon

247 to N&PL by more than ten-fold, reducing the Gibbs free energy of transition (DeltaG(O)) from 119 to

248 rformed calculations, according to which the Gibbs free energy of twin-free aragonite is close to tha

249 perativity parameter sigma ~6 x 10(-5) and a Gibbs free energy of unfolding of g(nu) ~100 cal/mol per

250 stability, measured as the difference in the Gibbs free energy of unfolding, between the wild-type an

251 hermal titration calorimetry showed that the Gibbs free energy of VEGF-A, VEGF-C, or VEGF-E binding t

252 ction and their contribution to the apparent Gibbs' free energy of tRNA binding.

253 ase of biochemical equilibrium constants and Gibbs free energies, originally designed as a web-based

254 hospholipid mass and approximately 20 cal of Gibbs free energy per gram wet weight of tissue).

255 The Gibbs free energy phase diagram as a function of electro

256 zed in solvolyses, despite the fact that the Gibbs free energy profile favors the strict SN1Ar proces

257 The computed Gibbs free energy profiles for E- and Z-isomers when (1)

258 round a single scaffold it is found that the Gibbs free-energy release upon binding is greater than c

259 It is suggested that the Gibbs free energy released as a result of the high-affin

260 parameters (change in enthalpy, entropy, and Gibbs free energy) revealed the nature of the main parti

261 phase transitions, the second derivatives of Gibbs free energy (specific heat and compressibility) di

262 inimum, which completely disappears from the Gibbs free energy surface.

263 gs provide an accurate and general theory of Gibbs free energy that can be validated experimentally b

264 From the B3LYP/6-31++G(3df,3pd) Gibbs free energy, the keto-enol tautomeric equilibrium

265 l electron acceptor, oxygen, and utilize the Gibbs free energy to transport protons across a membrane

266 ng the last two years, including addition of Gibbs free energy values for compounds and reactions; re

267 This is also reflected by the Gibbs free energy values for the transition states, Delt

268 Secondary structure and predicted Gibbs free energy values of the psbA 5' untranslated reg

269 stable polymorphs by shifting their relative Gibbs free energies via increasing the surface area-to-v

270 The change in Gibbs free energy was also found to be positive for RCM

271 as well as the entropic contribution to the Gibbs free energy without major impact on the structure