Thermodynamics. An Advanced Treatment for Chemists and Physicists

Guggenheim, E. A.

doi:10.1515/zna-1950-0413

Cited by 153 publications

(267 citation statements)

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“…The two enduring models of the interphase arise from J. Willard Gibbs [135] and E. A. Guggenheim [136]. Gibbs’ approach has great practical utility but is not as intuitive as that of Guggenheim.…”

Section: 0 Technical Backgroundmentioning

confidence: 99%

“…water and protein, respectively) according to the Guggenheim surface construction [29, 136] reads:

d γ = - true[Γ_{2} - true(\frac{n_{B, 2}}{n_{B, 1}} true) Γ_{1} true] d μ_{2} = - true(\frac{1}{a} true) true[n_{I, 2} - true(\frac{n_{B, 2}}{n_{B, 1}} true) n_{I, 1} true] d μ_{2}

where γ is interfacial energy (ergs/cm 2 = mJ/m 2 equivalent to interfacial tension, dyne/cm = mN/m) Γ ≡( n I / a ) measures the mole number within the interphase n I surrounding a unit area a of adsorbent (moles/cm 2 ), and n B is the mole number within bulk solution. The subscripts B and I track bulk solution and interphase, respectively.…”

Section: 0 Technical Backgroundmentioning

confidence: 99%

“…Phenomenological rate equations based on this energy-barrier idea seemed to accommodate experimental kinetics data and so the energy-barrier idea was generally accepted, even though this construction of the surface region invites a number of conceptual questions. Among these, why is it that a subsurface zone and an interfacial plane do not together constitute an interphase similar to that employed by Gibbs [135] and Guggenheim [136] in development of surface thermodynamics? And how is it that solute molecules collected in the subsurface zone do not qualify as adsorbed from solution and do not contribute to decay in interfacial tensions?…”

Section: 0 Revising the Research Paradigmmentioning

confidence: 99%

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Protein adsorption in three dimensions

2012

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Recent experimental and theoretical work clarifying the physical chemistry of blood-protein adsorption from aqueous-buffer solution to various kinds of surfaces is reviewed and interpreted within the context of biomaterial applications, especially toward development of cardiovascular biomaterials. The importance of this subject in biomaterials surface science is emphasized by reducing the “protein-adsorption problem” to three core questions that require quantitative answer. An overview of the protein-adsorption literature identifies some of the sources of inconsistency among many investigators participating in more than five decades of focused research. A tutorial on the fundamental biophysical chemistry of protein adsorption sets the stage for a detailed discussion of the kinetics and thermodynamics of protein adsorption, including adsorption competition between two proteins for the same adsorbent immersed in a binary-protein mixture. Both kinetics and steady-state adsorption can be rationalized using a single interpretive paradigm asserting that protein molecules partition from solution into a three-dimensional (3D) interphase separating bulk solution from the physical-adsorbent surface. Adsorbed protein collects in one-or-more adsorbed layers, depending on protein size, solution concentration, and adsorbent surface energy (water wettability). The adsorption process begins with the hydration of an adsorbent surface brought into contact with an aqueous-protein solution. Surface hydration reactions instantaneously form a thin, pseudo-2D interface between the adsorbent and protein solution. Protein molecules rapidly diffuse into this newly-formed interface, creating a truly 3D interphase that inflates with arriving proteins and fills to capacity within milliseconds at mg/mL bulk-solution concentrations CB. This inflated interphase subsequently undergoes time-dependent (minutes-to-hours) decrease in volume VI by expulsion of either-or-both interphase water and initially-adsorbed protein. Interphase protein concentration CI increases as VI decreases, resulting in slow reduction in interfacial energetics. Steady-state is governed by a net partition coefficient P=true(/CBCItrue). In the process of occupying space within the interphase, adsorbing protein molecules must displace an equivalent volume of interphase water. Interphase water is itself associated with surface-bound water through a network of transient hydrogen bonds. Displacement of interphase water thus requires an amount of energy that depends on the adsorbent surface chemistry/energy. This “adsorption-dehydration” step is the significant free-energy cost of adsorption that controls the maximum amount of protein that can be adsorbed at steady state to a unit adsorbent-surface area (the adsorbent capacity). As adsorbent hydrophilicity increases, protein adsorption monotonically decreases because the energetic cost of surface dehydration increases, ultimately leading to no protein adsorption near an adsorbent water wettability (surface energy) characterized ...

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Section: 0 Technical Backgroundmentioning

confidence: 99%

“…water and protein, respectively) according to the Guggenheim surface construction [29, 136] reads:

d γ = - true[Γ_{2} - true(\frac{n_{B, 2}}{n_{B, 1}} true) Γ_{1} true] d μ_{2} = - true(\frac{1}{a} true) true[n_{I, 2} - true(\frac{n_{B, 2}}{n_{B, 1}} true) n_{I, 1} true] d μ_{2}

Section: 0 Technical Backgroundmentioning

confidence: 99%

Section: 0 Revising the Research Paradigmmentioning

confidence: 99%

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Protein adsorption in three dimensions

2012

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“…We prefer the ideal gas notation, because tht: values specified do not depend on the: state of our knowledge of the virial coeff.cients of the gas. The best procedure, however, is to eliminate the source of confusion by expressing the amount of dissolved gas directly in pgatoms (or pmol) or mg. Other reasons for this choice are discussed by Helland-Hansen et al (1948) and Carpenter (1966). We have included the volume…”

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confidence: 99%

The concentration and isotopic fractionation of gases dissolved in freshwater in equilibrium with the atmosphere. 1. Oxygen

Benson

Krause

1980

Limnology & Oceanography

205

122

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Equations and tables are presented from which accurate values can be obtained, in any of several sets of units, for the concentration of oxygen dissolve11 in freshwater in equilibrium with the atmosphere from 0" to 40°C and 0.5 to 1.1 atm. The y are based on values for the Henry coefficient of oxygen, k,,, which have an estimated accuracy of 0.02%. Equations are derived which relate k, to equilibrium concentrations in natilral waters. The equations include corrections for molecular interactions in the vapor pha.;e. Uncertainty about the best way to correct for these interactions limits the estimated act Iracy of the derived values to about & 0.07% at 0°C and 0.04% at 4O"C, but the new results are much more accurate than values from the UNESCO tables. Within their random errors, previous measurements agree very well with the new results. Under equilibrium conditions, and between 0" and 6O"C, the per mil difference between the 340,:3202 abundance ratio in t le dissolved gas and the air is given by 6 = -0.730 + (427/T), where T is in kelvin and the standard deviation is <0.02%0.

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“…Pictet (1876) (see page 406 in [1] and page 128 in [2]) and Trouton (1884) [3] assumed from experimental data that the molar boiling entropy DS boil ¼ DH boil =T boil is constant, about ð10 À 11ÞR for all one-component systems (R: universal molar gas constant). Several attempts to explain that rule are known as well as explanations for deviations between experimental data and the expected value [4][5][6][7][8][9][10][11][12]. The rule of Pictet-Trouton has been tentatively explained recently again by the assumption that boiling occurs in corresponding states according to a claimed "corresponding states principle" without testing whether that rule is fulfilled at all [12].…”

Section: Introductionmentioning

confidence: 99%

Boiling of the Chemical Elements

Hoffmann

2004

Materialwissenschaft Werkst

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The molar boiling entropy, DS boil , has been assumed in the literature to be approximately the same for one-component systems, which is known as the rule of Pictet-Trouton. Using experimental data on DS boil of the chemical elements, however, this rule must be questioned. Instead, the increase of the molar entropy upon boiling is estimated from the expansion of the melt to the volume of the vapour under atmospheric pressure. This yields the right order of magnitude for DS boil .The molar boiling entropy depends on the number of electrons in the outermost electron shell of the free atoms of the chemical elements. Thus, the electronic system stores some entropy needed for boiling and seems to cause the phase transition liquid/vapour. This is supported by the correlation between the electron configuration and the molar specific heat capacities in the liquid and the vapour state near the boiling temperature. Accordingly, boiling is induced by electronic transitions into anti-bonding states at a rate sufficient to increase the partial pressure of the vapour within a melt. This is in contrast to the traditional explanation of boiling by breaking pair bonds between the atomic constituents of a melt which neglects the effect of transitions of the bonding electrons.Key words: liquid-gas transition, rule of Pictet-Trouton, boiling, boiling entropy, evaporation Nach der Regel von Pictet-Trouton wurde bisher in der Literatur angenommen, dass die molare Siedeentropie DS boil (molare Verdampfungsentropie bei der Siedetemperatur) für die Einkomponenten-Systeme näherungsweise konstant sei. An Hand experimenteller Daten chemischer Elemente muss jedoch diese Regel in Frage gestellt werden. Statt dessen wird die molare Siedeentropie aus der Volumenexpansion der Schmelzen in die Dampfphase unter Atmosphärendruck abgeschätzt. Hieraus ergibt sich die korrekte Grös-senordnung von DS boil .Die molare Siedeentropie hängt ausserdem von der Anzahl an Elektronen in der äusseren Schale der freien Atome der chemischen Elemente ab. Das Elektronensystem kann somit auch Entropie speichern und scheint für den Ü bergang Flüssigkeit/Dampf verantwortlich zu sein. Dies wird durch die Korrelation zwischen der Elektronenkonfiguration und den molaren spezifischen Wärmekapazitäten der Flüssigkeit und des Dampfes nahe der Siedetemperatur gestützt. Danach wird Sieden durch die äusseren Elektronen hervorgerufen, die mit hinreichenden Raten in Anti-bonding-Zustände übergehen, so dass innerhalb der Schmelze der Siededruck erreicht wird. Dies steht im Gegensatz zur bisherigen Beschreibung des Siedens, bei der ein Aufbrechen von Paarbindungen zwischen den atomaren Bausteinen der Schmelze angenommen wird und der Einfluss von Ü bergängen der Bindungselektronen vernachlässigt wird.

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Thermodynamics. An Advanced Treatment for Chemists and Physicists

Cited by 153 publications

References 0 publications

Protein adsorption in three dimensions

Protein adsorption in three dimensions

The concentration and isotopic fractionation of gases dissolved in freshwater in equilibrium with the atmosphere. 1. Oxygen

Boiling of the Chemical Elements

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