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1 ercentage of NACs is 0.16%, based on the 1 M standard state.
2 ty (free energy) in aqueous solutions at 1 M standard state.
3 ients depends on the concentration units and standard states.
4 igh energy barrier between the remodeled and standard states.
5 imer-->two random coil monomers) to obtain a standard-state (1M) melting temperature for each variant
6 ansition is 24 +/- 2 kcal mol-1, both at 1 M standard state and pH 7.5.
7 lution in different concentration scales and standard states and its effect on our subsequent analysi
8 free energies of Xe, Kr and Ar relative to a standard state at a pressure of 1 bar.
9  the remodeled state is less stable than the standard state but that the remodeled state is kinetical
10        A specific distribution of compounds' standard-state changes of enthalpy and entropy between m
11  energetics of all receptors under a single "standard state" condition.
12 d 45.0 +/- 2.5 kcal/mol, respectively, under standard state conditions (1 M hexamer) as compared to a
13  at pH 8.5 to be 68.7 +/- 3.2 kcal/mol under standard state conditions (1 M hexamer).
14  of folding in the absence of urea and under standard state conditions of 14.1 +/- 0.2 kcal mol-1, 7.
15  and tabulating thermodynamic data; however, standard state conventions and appropriate reference sta
16     These measurements yield the barrier and standard state enthalpies, entropies, and free energies
17 ut has been associated with large changes in standard-state enthalpy (DeltaH(o)) and entropy (DeltaS(
18                                          The standard-state enthalpy of formation from the elements (
19 st involve an unusually large conformational standard-state enthalpy, DeltaH(o): positive DeltaH(o) f
20                                      Through standard-state equilibrium measurements and advanced com
21                         Finally, we define a standard state for DNA melting, the temperature at which
22 ises from the fact that extrapolation to the standard state free energy change normalizes the statist
23                    The second component is a standard state free energy change, which informs on the
24 ggesting that this conformation is of higher standard state free energy than that of the free recepto
25 te building blocks are used so that the AlB2 standard-state free energy is low enough to overcome the
26  the most complete level of theory the 173 K standard-state free energy of dimerization of fluorometh
27 xamined in this study function to reduce the standard-state Gibbs free energy of reaction for deproto
28 For one translational/rotational unit at 1 M standard state in aqueous solution, the results for enth
29                         The free energies at standard state in the absence of denaturant for Trp19/L3
30                           The free energy at standard state in the absence of denaturant was estimate
31 oid is modestly destabilizing, relative to a standard state in water, and that this destabilization i
32  folding in the absence of denaturant and at standard state is -20.37(+/- 1.04) kcal (mol dimer)(-1).
33  that pin_hic is more efficient than current standard state-of-art tools, and it can generate much mo
34 al simulations, and a direct comparison with standard state-of-the-art EEG analysis in a well-establi
35                                              Standard state-of-the-art techniques for screening of el
36               This QIS was fabricated with a standard, state-of-the-art CMOS process with 2-layer waf
37 y-Fe(III) reduction correlated well with the standard state reduction potential at pH 7.0 (E degrees
38 e energetics should be based on the Ben-Naim standard state (solute transfer between fixed positions
39 diate (I2) of 4.3 kcal/mol while the overall standard state stability of the native homodimer relativ
40 ibrium constants, and they may also serve as standard states that are convenient for organizing and t
41 mum stability (T(S); 6-10 degrees C), yields standard-state thermodynamic functions (deltaG(o)(obs),
42                            By redefining the standard state to a lower, more physiological protein co