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

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

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

5 conformation changes that contribute to the Gibbs free energy.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

35 The Gibbs free energy change for denaturation of the protein

36 (2+), Br(-)](+*) was due to a less favorable Gibbs free energy change for electron transfer that resu

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

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

39 The Gibbs free energy change for reactions of inactivation o

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

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

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

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

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

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

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

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

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

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

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

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

52 Gibbs free energy changes of reaction were calculated to

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

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

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

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

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

58 Gibbs free energy contribution values were estimated for

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

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

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

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

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

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

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

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

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

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

69 The Gibbs free energy difference between native and unfolded

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

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

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

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

74 Gibbs free energies for solute transfers from gas to ret

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

103 27-Mg (Mg-MOF-74), ab initio calculations of Gibbs free energies of adsorption have been performed.

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

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

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

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

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

109 The Gibbs free energies of oxygen transfer from these hetero

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

111 Gibbs free energies of reaction depended on the net char

112 The highest Gibbs free energies of reaction for physical adsorption

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

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

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

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

117 Gibbs free energies of reactions with various free radic

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

143 5 A of the phosphorylation site--encode the Gibbs free energy of inhibition (DeltaG(inhibition)) for

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

145 The Gibbs free energy of mixing dissipated when fresh river

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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