THERMODYNAMICS– PHYSICALCHEMISTRYOF AQUEOUSSYSTEMS EditedbyJuanCarlosMoreno‐Piraján Thermodynamics – Physical Chemistry of Aqueous Systems Edited by Juan Carlos Moreno-Piraján Published by InTech Janeza Trdine 9, 51000 Rijeka, Croatia Copyright © 2011 InTech All chapters are Open Access articles distributed under the Creative Commons Non Commercial Share Alike Attribution 3.0 license, which permits to copy, distribute, transmit, and adapt the work in any medium, so long as the original work is properly cited. After this work has been published by InTech, authors have the right to republish it, in whole or part, in any publication of which they are the author, and to make other personal use of the work. Any republication, referencing or personal use of the work must explicitly identify the original source. Statements and opinions expressed in the chapters are these of the individual contributors and not necessarily those of the editors or publisher. No responsibility is accepted for the accuracy of information contained in the published articles. The publisher assumes no responsibility for any damage or injury to persons or property arising out of the use of any materials, instructions, methods or ideas contained in the book. Publishing Process Manager Viktorija Zgela Technical Editor Teodora Smiljanic Cover Designer Jan Hyrat Image Copyright Andrejs Pidjass, 2010. Used under license from Shutterstock.com First published September, 2011 Printed in Croatia A free online edition of this book is available at www.intechopen.com Additional hard copies can be obtained from orders@intechweb.org Thermodynamics – Physical Chemistry of Aqueous Systems, Edited by Juan Carlos Moreno-Piraján p. cm. ISBN 978-953-307-979-0 free online editions of InTech Books and Journals can be found at www.intechopen.com Contents Preface IX Chapter 1 Thermodynamics of Molecular Recognition by Calorimetry 1 Luis García-Fuentes, Ramiro, Téllez-Sanz, Indalecio Quesada-Soriano and Carmen Barón Chapter 2 Theory and Application of Thermoelectrochemistry 27 Zheng Fang Chapter 3 Thermodynamics and the Glass Forming Ability of Alloys 49 Chengying Tang and Huaiying Zhou Chapter 4 Information Thermodynamics 73 Bohdan Hejna Chapter 5 Mesoscopic Thermodynamics in the Presence of Flow 105 I. Santamaría-Holek, R. Lugo-Frías, R. F. Rodríguez and A. Gadomski Chapter 6 Non-Instantaneous Adiabats in Finite Time 131 Delfino Ladino-Luna and Ricardo T. Páez-Hernández Chapter 7 Heterogeneous Melting in Low-Dimensional Systems and Accompanying Surface Effects 157 Dmitry G. Gromov and Sergey A. Gavrilov Chapter 8 Pressure Effects on Thermodynamics of Polymer Containing Systems 191 Shichun Jiang and Hongfei Li Chapter 9 Potential-pH Diagrams for Oxidation-State Control of Nanoparticles Synthesized via Chemical Reduction 223 Shunsuke Yagi VI Contents Chapter 10 On the Extremum Properties of Thermodynamic Steady State in Non-Linear Systems 241 Gy. Vincze and A. Szasz Chapter 11 Thermodynamic Study of Grinding-Induced Loratadine Inclusion Complex Formation Using Thermal Analysis and Curve-Fitted FTIR Determination 317 Shan-Yang Lin, Hong-Liang Lin, Chih-Cheng Lin, Cheng-Hung Hsu, Tieh-kang Wu and Yu-Ting Huang Chapter 12 Three-Dimensional Constitutive Viscoelastic Model for Isotropic Materials 327 Donald Picard and Mario Fafard Chapter 13 Hydrogen Bond Interactions Between Water Molecules in Bulk Liquid, Near Electrode Surfaces and Around Ions 351 Abhishek Rastogi, Amit K. Ghosh and SJ Suresh Chapter 14 The Stability of a Three-State Unfolding Protein 365 Yang BinSheng Chapter 15 Phase Diagram and Waterlike Anomalies in Core-Softened Shoulder-Dumbbell Complex Fluids 391 Paulo A. Netz, Guilherme K. Gonzatti, Marcia C. Barbosa, Juliana Z. Paukowski, Cristina Gavazzoni and Alan Barros de Oliveira Chapter 16 Effect of Magnetic and Mechanical Fields on Phase Liquid Crystalline Transitions in Solutions of Cellulose Derivatives 407 S. A. Vshivkov Preface Thermodynamics is one of the most exciting branches of physical chemistry which hasgreatlycontributedtothemode rnsci enc e.Sinceitsincepti o n, greatmindsha ve built their theories of thermodynamics. One should name those of Sadi Carnot, Clapeyron Claussius, Maxwell, Boltzman, Bernoulli, Leibniz etc. Josi ah Will ard Gibbs had perha ps the greates t sc ientific influence on the development of thermodynamics.Hisattentionwas forsometimefocused onthestudyof theWatt steam engine. Analysing the balance of the machine, Gibbs began to develop a method for calculating the variables involved in the processes of chemical equilibrium. He deduced the phase rulewh ich determines the degrees of freedom of a physicochemical system based on the number of system components and the numberofphases.Healsoidentifiedanewstatefunctionofthermodynamicsystem, theso‐calledfreeenergyorGi bbsenergy(G),whichallo ws spontaneityandensures aspecificphysicochemicalprocess(suchasachem icalreactionorachangeofstate) experienced by a system without interfering with the enviro nme nt around it. The essential feature of ther modyn amics and the differenc e betw ee n it and other branchesofscienceisthatitincorporates theconceptofheatorthermalene rgyasan important part in the en ergy systems. The nature of heat was not always clear. Today we know that the random motion of molecules is the essence of heat. So me aspects of thermodynamics are so general and deep that they even deal with philosophical issues. These issues also deserve a deeper considera tio n, before tacklingth etechnicaldetails.Thereasonis asi mpl eone‐beforeonedoesanything, onemustunders tandwhattheywant. Inthepast,historians consideredthermodynamicsasasciencethatisisolated, butin recent years scientists have incorporated more friendly approach to it and have demonstratedawiderangeofapplicat ionsofthermodynamics. These four volumes of applied thermodynamics, gathered in an orderly manner, presentaseriesofcontributionsbythefinestscientistsintheworldandawiderange of applications of thermodynamics in various fields. These fields include the environmental science, mathematics, biology, fluid and the materials science. These four volumes of thermod ynamics can be used in post‐graduate courses for students and as reference books, since they are written in a language pleasing to the reader. X Preface They can also serve as a reference material for researchers to whom the thermodynamicsisoneoftheareaofinterest. JuanCarlosMoreno‐Piraján DepartmentofChemistry UniversityoftheAndes Colombia [...]... 100 -1 Power (µcal s ) 0 -1 -2 -4 0 kcal/mol of ligand kcal/mol of ligand -3 0 -8 -1 2 0 2 -4 -8 -1 2 -1 6 0 1 2 3 4 5 [S-hexylGSH]/[wild-type] 4 6 [S-hexylGSH]/[Y49F] Fig 8 Representative isothermal titration calorimetry measurements of the binding of ShexylGSH to the Y49F mutant of hGST P 1-1 A 15.32 μM mutant enzyme solution was titrated with 1.12 mM S-hexylGSH (inset) Integrated heats per mol of S-hexylGSH... Y49F GSH GSH S-hexylGSH S-hexylGSH K M-1 11630302 388383 (8.10.3)·105 (4.30.1)·105 H TSo kcal mol-1 -1 1.210.12 -5 .650.12 -1 3.040.14 -9 .170.14 -1 6.130.07 -8 .040.07 -1 7.140.08 -9 .450.08 Cpo cal K-1 mol-1 -2 94.22.7 -1 99.526.9 -4 41.648.7 -3 33.628.8 Table 2 Thermodynamic parameters for the interaction of GSH and S-hexylGSH to the Y49F mutant and wild-type enzymes of hGST P 1-1 , at 25.2ºC... properly Time (min) 0 30 60 90 0 120 150 -1 -2 µcals µcal s 0 -5 -1 0 -4 -1 0 0 0 kcal/mol of EASG kcal/mol of GSNO Time (min) 100 200 300 -2 -4 -6 0 10 20 30 40 [GSNO]/[wtGST] 50 -6 -1 2 -1 8 -2 4 0 2 4 6 [EASG]/[C47S] Fig 2 Representative isothermal titration calorimetry measurements for the binding at 25.1 °C of GSNO (left panel) and EASG (right panel) to wt-hGSTP 1-1 and its C47S mutant, respectively Solid... Mes, Hepes and TES buffers 16 Thermodynamics – Physical Chemistry of Aqueous Systems 12 4 -4 0 Hobs (kcal·mol-1) -1 Heat Flux (cal s ) 8 -4 -8 -8 -1 2 -1 6 -1 2 0 15 30 Time (min) 45 0 2 4 6 8 Hioniz (kcal·mol-1) Fig 7 Protonation effect in the dUTP hydrolysis by PfdUTPase at pH 7 and 25 ºC The calorimetric thermograms correspond to one 20 L injection of 9.98 mM dUTP to the calorimetric cell containing... 2 B -1 -2 -3 A -1 C 0 200 400 600 Time (s) 0 -1 D 160 800 -1 v (nM·s ) Heat Flux (µcal·s ) 1 cal·s -1 0 120 80 40 -2 0 0 10 20 30 40 50 [dUTP] (M) -3 0 20 40 60 Time (min) Fig 3 PfdUTPase-catalyzed hydrolysis of dUTP in 25 mM MES, 100 mM NaCl, 25 mM MgCl2, 1 mM β-mercaptoethanol at pH 7 and 25 °C (A) Typical calorimetric trace (μcal/s versus time) obtained after addition of three injections of 5... Kd (µM) ΔH (kcal mol-1) TΔS0 (kcal mol-1) ΔC0p (cal mol-1K-1) WT 0.5 ± 0.1 -1 4.17 ± 0.37 -5 .59 ± 0.37 -2 64 ± 24 Y108V 0.3 ± 0.1 -1 3.34 ± 0.46 -4 .55 ± 0.31 -4 15 ± 17 Table 3 Thermodynamic parameters of the interaction of EASG with wt GST P 1-1 and theY108V mutant at 25 oC and pH 7.0 Therefore, these results demonstrate that ITC measurements can provide a thermodynamic fingerprint of drug–protein interactions,... of a linear plot 18 Thermodynamics – Physical Chemistry of Aqueous Systems according to Eq 29 (Table 1) A negative slope was obtained (nH< 0), with nH ~-0 .44 and nH ~-0 .11 for the binding of GSH to the wild type enzyme and its Y49F mutant, respectively (Table 1) Hioniz (kcal mol-1) Phosphate 1.22 Mes 3.72 Mops 5.27 Aces 7.53 nH Buffer Y49F mutant GSH S-hexylGSH - Hobs (kcal mol-1) 13.04 0.31 17.14... 111 ring planes aS-2-iodobenzylglutathione from the PDB structure 1M9B b wt Tyr 111 cPhe 111 24 Thermodynamics – Physical Chemistry of Aqueous Systems The predicted S-benzylglutathione binding modes agree with the crystallographic structure for this reference ligand (Table 4), where the aromatic ring of the benzyl moiety stacks between the side-chains of Tyr 104 and Tyr 111 in the case of the wt and the... demonstrated that EA (inhibitor and substrate of hGSTP 1-1 ) binds irreversibly to the 2 loop Cys 47 Fig 5 shows a representative thermogram Time (min) 0 60 120 180 240 0.0 -1 -0 .5 -1 .0 cal s -1 Power (µcal· s ) 0.0 -0 .1 -0 .2 -1 .5 0 3 6 9 Time (min) 12 Fig 5 Calorimetric thermogram for the titration of 23 µM wt GSTP 1-1 with 5 µL injections (1 µL first injection) of 2.1 mM EA in 20 mM sodium phosphate, 5... 20 Thermodynamics – Physical Chemistry of Aqueous Systems As shown in Fig 9, although ΔG0 is almost insensitive to the change in temperature, ΔH and TΔS0 strongly depend on it, for both enzymes This feature is known as enthalpy-entropy compensation, and it is very common in most of the thermodynamic binding studies of biological systems The enthalpy-entropy compensation is related to the properties of . THERMODYNAMICS – PHYSICAL CHEMISTRY OF AQUEOUS SYSTEMS EditedbyJuanCarlosMoreno‐Piraján Thermodynamics – Physical Chemistry of Aqueous Systems Edited. 02468 -2 0 -1 5 -1 0 -5 0 -3 -2 -1 0 0 100 200 300 400 Time (min) Power (µcal s -1 ) [dUDP]/[dUTPase] kcal/mol of dUDP H K a n Fig. 1. Scheme of the calorimeter reaction cell (left) and results of. 6·10 5 M -1 , with a stoichiometry of 3 mol of ligand per mol of trimeric enzyme, a concentration of macromolecule of approximately 20 µM yields a C-value of 36, within its ideal 1 0-1 00 range.