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1 om measured thermodynamic quantities such as heat capacity.
2 cooler Earth-by exploiting transition-state heat capacity.
3 increase with increasing heat diffusion and heat capacity.
4 easurements reveal a clear transition in the heat capacity.
5 y and an approximate, homogeneous volumetric heat capacity.
6 nteraction, they do not affect the change in heat capacity.
7 f polar compounds, which cause a decrease in heat capacity.
8 nd associated with large negative changes in heat capacity.
9 from accessible surface area (ASA) models of heat capacity.
10 rimed-template DNA with significant negative heat capacities.
11 of ions or oils entails large entropies and heat capacities.
12 gy, bulk/shear moduli, Debye temperature and heat capacities.
13 tructurally distinct and have very different heat capacities.
14 e observed changes in enthalpy, entropy, and heat capacity accompanying the F --> I and I --> U trans
16 e outliers show anomalously large changes in heat capacity, an indicator of conformational change or
18 "calorimeter on a chip") are used to measure heat capacities and phase transition enthalpies for thin
23 IR) correlation spectroscopy, the change in heat capacity and enthalpy of denaturation by differenti
24 methanol is highly volatile and has a lower heat capacity and enthalpy of vaporization than water.
25 ally separated to obtain simultaneously both heat capacity and expansibility in continuous DSC temper
26 hat it is possible to measure simultaneously heat capacity and expansibility of biomolecules in a sin
28 es, the model gives good predictions for the heat capacity and helicity versus temperature and urea.
29 rcooled liquid, many quantities, for example heat capacity and isothermal compressibility kappaT, sho
30 litated by the combination of low electronic heat capacity and large plasmonic field concentration in
32 physical reason for the opposite changes in heat capacity and new insight into water structure aroun
33 t Mie theory reveal that both the electronic heat capacity and the electron-phonon coupling constant
34 evidence, including dielectric permittivity, heat capacity and thermal conductivity measured down to
35 tion of temperature that is due to the large heat capacity and thermal conductivity of honey relative
37 sorption of light-because its small electron heat capacity and weak electron-phonon coupling lead to
39 erturbations ( approximately 64% increase in heat capacity), and is resistant to Ostwald ripening.
40 e protein has an unusually high native-state heat capacity, and consequently, the change in heat capa
42 nd DeltaF(T)--the folding enthalpy, entropy, heat capacity, and free energy--as functions of temperat
43 present the structure, transport properties, heat capacity, and magnetization of single-crystal Gd(11
44 susceptibility, pulsed-field magnetization, heat capacity, and muon-spin relaxation) and electronic
45 er's isothermal compressibility and isobaric heat capacity, and the magnitude of its thermal expansio
47 re is a corresponding jump in the calculated heat capacity as well as in the temperature derivative o
49 t the relative enthalpic and entropic terms, heat capacity, association rates, and activation energy
50 d that upon complex formation, the change in heat capacity at constant pressure, DeltaC(p), was negat
53 uctivity plateau and the "boson peak" in the heat capacity at moderately low temperatures are directl
55 iscrepancies between observed and calculated heat capacities based on buried surface area changes in
57 that have been previously shown to influence heat capacity, bridging water molecules in a highly pola
58 tation, increases with increasing electronic heat capacity, but decreases with increasing electron-ph
59 n and water binding to the overall change in heat capacity by means of a series of site-directed muta
60 taHf(degrees), entropies (S(degrees)298, and heat capacities (C(degrees)p obtained from B3LYP/6-31G(d
62 es and states are determined by matching the heat capacity calculated through Monte Carlo simulations
63 for some anomalous ligands, large changes in heat capacity can apparently substitute for a lack of st
64 n expected binding enthalpy and the positive heat capacity can be explained by a temperature dependen
65 rhenius plots are explained by the change in heat capacity caused by the binding of waters in an inva
67 anine nucleotide is characterized by a large heat capacity change (-621, -467, -235, and -275 cal x m
68 A complexation is associated with a negative heat capacity change (Delta C(p)), the magnitude of whic
69 , entropy change (DeltaS = -0.110 kJ/mol/K), heat capacity change (DeltaC(p) = -7.6 kJ/mol/K), the en
73 orrelated with the protein size and with the heat capacity change (DeltaC(p)) but is positively corre
75 of these studies suggest that the intrinsic heat capacity change (DeltaC(p)) for the binding of paro
77 y change of interaction, a constant-pressure heat capacity change (DeltaC(p)) of the interaction was
79 may be due to greater uncertainties in their heat capacity change (DeltaC(p)) values, a weaker hydrop
81 characterized by a positive enthalpy, small heat capacity change (DeltaC(p)= -33 kcal mol(-1)), and
83 thalpy change (DeltaH(obs)) and the negative heat capacity change (DeltaC(p,obs)) for Escherichia col
84 tions were characterized by a large negative heat capacity change (DeltaC(P,obs)), approximately half
89 nding complex with the most negative binding heat capacity change (DeltaG = approximately -13 kcal mo
90 .8 kcal/mol at 25 degrees C), and a negative heat capacity change [DeltaC(p)() = -165 cal/(mol K)].
94 owever, there is almost no difference in the heat capacity change for binding of the NADP(+) to the C
98 rmal titration calorimetry measurements, the heat capacity change for the reaction is -256 +/- 10 cal
100 e fact that this break does not occur in the heat capacity change function for formation of the highe
101 seem to infer that because the break in the heat capacity change function for the lower affinity bin
104 dependence of ATP binding indicated that the heat capacity change is small, whereas the binding of GS
105 binding enthalpy by ITC revealed a negative heat capacity change larger than expected from surface b
106 ributions, the temperature dependence of the heat capacity change needs to be explicitly taken into a
108 temperature over this range with an average heat capacity change of -94 Jmol(-1)K(-1) for the three
109 ases with temperature, displaying a positive heat capacity change of 194 +/- 7 cal K(-)(1) mol(-)(1)
110 an also contribute substantially to negative heat capacity change on formation of a protein-DNA compl
111 from 5 to 45 degrees C, suggesting that the heat capacity change on helix formation is very small.
112 ted solely to this change in water, then the heat capacity change per incorporated water is almost th
114 unction of temperature indicating a negative heat capacity change that is typical for DNA minor-groov
115 -type-specific complexes with respect to the heat capacity change upon binding (C degrees P), the cha
124 resence of melibiose yields a large negative heat capacity change; in addition, the conformational en
127 I, respectively, with a 2-fold difference in heat capacity changes (-604 versus -331 cal mol(-1) K(-1
129 aromomycin amino groups, as well as positive heat capacity changes (deltaC(p)) for three of the five
130 each residue enabled assessment of the local heat capacity changes (DeltaC(p)) from ligand binding.
134 mplex with one of the least negative binding heat capacity changes (DeltaG = approximately -8.5 kcal
135 and the magnitudes of enthalpy, entropy and heat capacity changes all decrease strongly with increas
136 es C show significant enthalpy, entropy, and heat capacity changes associated with both Na(+) binding
139 t denaturant kinetic m-values and activation heat capacity changes for 13 proteins to determine amoun
145 d 2-methyl-2,4-pentanediol, the enthalpy and heat capacity changes indicate that the complex with wea
146 the unfavorable binding entropies and large heat capacity changes measured for many other TCR-ligand
147 companied by a significant difference in the heat capacity changes observed for binding the two ligan
149 temperature dependent, with negative binding heat capacity changes ranging from -800 to -271 cal mol(
151 rotein complexes can be explained largely by heat capacity changes that would result solely from fold
152 analogs were compared, and the enthalpy and heat capacity changes upon denaturation were determined
153 ding the first experimental estimate for the heat capacity changes upon helix-coil transition, DeltaC
158 sociated with an enhanced negative change in heat capacity consistent with conformational changes in
159 a significant portion of binding energy and heat capacity could be assigned to structural reorganiza
160 to Gibbs free energy, enthalpy, entropy, and heat capacity could be distinguished by applying additiv
161 eters are fixed by simultaneously fitting to heat capacity curves for histidine binding protein and u
162 as been successful in calculating the excess heat capacity curves, the fluorescence recovery after ph
163 i.e. duplex formation results in a constant heat capacity decrement, identical for CG and AT pairs.
164 e adduct incurred a large negative change in heat capacity DeltaC(p)(o)(obs) (-1.1 kcal mol(-1) K(-1)
167 minal domain of NFU yields a change in molar heat capacity (DeltaC(p) approximately 138 cal mol(-1) K
169 and occurs with a large, positive change in heat capacity (DeltaC(P) degrees ) for both actomyosin V
170 ; however, changes in enthalpy, entropy, and heat capacity (DeltaC(p)) contribute differently to form
171 ical correlations have shown that changes in heat capacity (DeltaC(P)) scale linearly with the hydrop
172 n be associated with a significant change in heat capacity (deltaC(p)), this parameter is typically o
173 interaction, coupled with the large negative heat capacity (deltaC(p)=-0.67 kcaldeg(-1)mol(-1)), is c
177 is accompanied by a large negative change in heat capacity (deltaCp) arising from the total change in
179 , which entailed (1) measuring the change in heat capacity (DeltaCp) upon association, to assess the
180 ), the last given by an associated change in heat capacity (DeltaCp), can determine a channel's tempe
184 ements, make very little contribution to the heat capacity difference between folded and unfolded sta
186 in salt concentration, indirectly yielding a heat capacity effect, and the magnitude of this effect w
187 groove is entirely enthalpic with a negative heat capacity effect, i.e., is due to sequence-specific
188 ith an enthalpy close to zero and a negative heat capacity effect, while NSS are formed with a very p
190 analyzing this data for temperature-variable heat capacity effects (DeltaDeltaCp), and have similarly
191 taq polymerase demonstrate that the observed heat capacity effects are not the result of a coupled fo
194 e dependence to the high positive values for heat capacity, enthalpy, and entropy of wCp149 assembly.
196 inine methylation, a more negative change in heat capacity for folding, and a modest decrease in enth
199 rate) versus temperature plot (the change in heat capacity for the system, DeltaCPdouble dagger).
200 he energetic profile (enthalpy, entropy, and heat capacity) for both the ion-protein and nucleotide-p
202 folding as judged by DeltaCp, the change in heat capacity, found from the free energy change for hea
203 heoretical model is proposed to describe the heat capacity function and the phase behavior of binary
204 rees C thermal transition seen in the excess heat capacity function as monitored by differential scan
207 DeltaCp directly from the difference between heat capacity functions of the native and unfolded state
210 glass transition is much less feeble, with a heat capacity increase at Tg,2 about five times as large
211 lar surfaces of bases is responsible for the heat capacity increment on dissociation and, therefore,
214 of the cumulative density of states and the heat capacity indicates that there are still gaps betwee
219 iques are capable of providing variations in heat capacity, mass and average bulk composition of mate
222 mol% cholesterol is a linear function of the heat capacity measured by differential scanning calorime
223 in partially dried seeds are calculated from heat capacities, measured using differential scanning ca
224 detail on the basis of magnetic measurement, heat capacity measurement and neutron powder diffraction
226 erature-dependent electrical resistivity and heat capacity measurements reveal a bulk superconducting
227 c magnetic susceptibility and variable field heat capacity measurements show that F4BImNN acts as a q
232 s in the ac susceptibility, M vs H plots, or heat capacity mitigates against long-range order in 1alp
233 simulations, we reproduce the size-sensitive heat capacities of Al(N) clusters with N around 55, whic
235 a temperature resolution of 0.125 mK, a low heat capacity of 1.2 nJ mK(-1), and a rapid (unfiltered)
236 ood agreement of calculated and experimental heat capacity of 21 liquids, including noble, metallic,
237 havior and a temperature-dependent enthalpy (heat capacity of 610 +/- 84 cal/Mol K), is slowed in the
238 ere, combining the high absorptivity and low heat capacity of a nanoengineered plasmonic thin-film ab
243 enthalpy for poly(dA-dT)2 indicates a large heat capacity of binding of -705(+/-113) cal/molK, consi
244 rates how thermal analysis of changes in the heat capacity of blood serum proteins can provide an ins
245 gation of electron-ion coupling and electron heat capacity of copper in warm and dense states are pre
246 DeltaS is a result of the positive change in heat capacity of DNA upon melting, which we determine fr
247 rovided by the large and negative activation heat capacity of k(a)[DeltaC(o,++)(a)= -1.5(+/-0.2)kcal
249 the view that the major contribution to the heat capacity of protein solutions largely arises from l
250 tability increased by over 30 degrees C; the heat capacity of protein unfolding was estimated from th
251 deltaCp(o)(T)(reaction) (change in specific heat capacity of reaction at constant pressure) leads to
253 sult for frontogenesis is that the effective heat capacity of the surface water depends on mixed laye
256 from this thermodynamic data depends on the heat capacity of transfer as the sole parameter needed t
257 f one more parameter set to give the correct heat capacity of unfolded barnase in solution, it is pos
258 thalpy, denaturant dependence (m-value), and heat capacity of unfolding (DeltaC(p)()) of around 50% e
260 n the unfolded state, which results in a low heat capacity of unfolding (DeltaCp) relative to ecRNH.
261 correlation between compressibility and the heat capacity of unfolding infers a link between compres
264 at low concentrations of denaturant shows no heat capacity peak during thermal denaturation, indicati
266 ng rates, free energies, folding enthalpies, heat capacities, Phi-values, and temperature-jump relaxa
267 eat capacity of binding agrees well with the heat capacity predicted from 65% of the surface buried o
268 binding occurs with a positive change in the heat capacity, presumably reflecting a nucleotide-induce
269 temperature T(m) = 339 K extracted from the heat-capacity profile was in close agreement with the ex
271 present a detailed thermodynamic analysis of heat capacity profiles of membranes in the presence of a
273 endent synchrotron powder X-ray diffraction, heat capacity, Raman spectroscopy, and positron annihila
276 ave been used to characterize the changes in heat capacity, solvent-accessible surface, and hydration
279 s show strong curvature, and hence require a heat capacity term, DeltaC(p)(double dagger), to obtain
280 ndefinite increase at low temperature in the heat capacity, the compressibility, and the coefficient
281 gnetoresistance), magnetic measurements, and heat capacity, the ordering temperatures (TCDW) observed
282 ta to the pressure dependence of the partial heat capacity to examine the impact of protein stabilizi
283 The equilibrium data consist of the excess heat capacity, tryptophan fluorescence quantum yield, an
287 ises in part from an unusually low change in heat capacity upon unfolding (DeltaC(p)) for the thermop
289 at capacity, and consequently, the change in heat capacity upon unfolding is much lower than that exp
296 anges in enthalpy, entropy, free energy, and heat capacity, were found to be identical for the two pr
298 the chemical potential, the entropy, and the heat capacity, which displays a characteristic lambda-li
299 is accompanied by a large negative change in heat capacity without substantial modification of RNA st
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