II. The influence of temperature and adsorbed salts on the D.C. conductivity of polar polymer adsorbate systems

King, George E.; Medley, J. A.

doi:10.1016/0095-8522(49)90029-x

Cited by 26 publications

(14 citation statements)

References 9 publications

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“…Numerous investigators have shown that impurity ions in hygroscopic solids participate in the conduction process [17, 21,28,29]. However, in some experiments washing procedures were used to remove impurities [3,26] without changing the strong dependence of C on R.…”

Section: The Conduction Mechanismmentioning

confidence: 99%

A New Model of DC Conductivity of Hygroscopic Solids

Christie¹,

Woodhead²

2002

Textile Research Journal

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We investigate the DC conductivity of cotton, viscose, and wood and develop a quantitative theory. We propose that conduction occurs by exchange of protons within a hydrogen-bonded network of water molecules, in a manner analogous to that in liquid water and ice. According to this model, the very strong dependence of conductivity on regain, which is characteristic of these materials, arises from its dependence on the average distance between adjacent water molecules. We derive expressions for DC conductivity as a function of regain, which provide very good agreement with experimental data. With independent experimental evidence, we confirm a prediction by the theory that a similar conduction process occurs in dry cellulose.

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Section: The Conduction Mechanismmentioning

confidence: 99%

A New Model of DC Conductivity of Hygroscopic Solids

Christie¹,

Woodhead²

2002

Textile Research Journal

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“…Also, leaving aside at present the possibility ofelectronic conduction, the proton, with its radius that is smaller than that ofany other ion by a factor of105, should rank as the most mobile charged particle in a protein matrix. Evidence for protonic conduction in proteins includes that for keratin (20), cytochrome c and hemoglobin (21), collagen (22), and most recently for single crystals of lysozyme (23). Regarding the proton fluctuation model of Kirkwood and Shumaker (17) and its possible relevance to the low-frequency dispersion of Fig.…”

mentioning

confidence: 99%

Water structure-dependent charge transport in proteins.

Gascoyne¹,

Pethig²,

Szent‐Györgyi³

1981

Proc. Natl. Acad. Sci. U.S.A.

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Dielectric and conductivity measurements are reported for bovine serum albumin as a function of hydration. Strong evidence is found for the existence ofmobile charges whose short-and long-range hopping motion strongly depends on the physical state of the protein-bound water. These charges are considered to be protons. Insights into the nature of the electrical properties of protein-methylglyoxal complexes are provided, and the possibilities for correlated proton-electron motions are outlined.Modern biology is a molecular biology. The rates of most biological reactions are assumed to be limited by the classical concepts of mass action theories applicable to reacting molecules in solution. The main bearers oflife are the protein macromolecules, which are often to be found incorporated into membrane structures. This situation would appear to violate the physical basis ofclassical mass action theories and suggests that the functioning of such structural proteins is controlled at the submolecular level. The reactivity and subtlety that characterizes living systems also indicates that at its most fundamental level the "living state" operates at the submolecular level of nuclei and electrons (1). Such considerations ofthe reactivity of living systems led one of us to suggest nearly 40 years ago that the functioning of proteins should be understood by considering their submolecular properties. It was envisaged that one manifestation of such submolecular processes would be the ability of proteins to sustain electrical conductivity (2). However, as shown by the pioneering studies ofEley (3, 4), proteins isolated in their pure and dry condition are poor conductors. The basic reason for this is that the valence and conduction levels of extended electronic states of protein structures are separated by such a wide energy gap that at normal temperatures there is a negligible probability for the intrinsic generation of mobile charge carriers. Formation of charge-transfer complexes with electron-accepting molecules makes it possible for the electronic ground states ofa protein to become desaturated ofelectronic charge and lead to a conductivity sustained by positively charged electron "holes." Similarly, a charge-transfer interaction with an electron donor could result in the appearance of mobile electrons in the protein's conduction energy levels. The possibility that proteins can be so converted from insulators into conductors has been demonstrated by Eley and coworkers (5, 6) in conduction studies on complexes ofbovine plasma albumin with chloranil or chlorophyll, and our own studies (7-9) indicate the possibility that aldehydes such as methylglyoxal can act as electron acceptors in charge-transfer interactions with proteins. We believe that it is through such charge transfer that structural proteins are imbued with a submolecular reactivity that is essential for their full biological functioning.Our attempts to fully understand the basic process by which methylglyoxal, when incorporated into a protein's structure, in...

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“…Our data indicate that the charge carriers on the wet protein surface are protons. This view is also 4 held by many other investigators, notably King and Medley, Cardew 5 6 7 8 and Eley, Fuoss, lRiehl, and Taylor. These investigators reached their conclusions by studies of dc conductivity measurements.…”

Section: Objectives Of the Investigationmentioning

confidence: 58%

The Dielectric Properties of Water and Their Role in Enzyme-Substrate Interactions

Vogelhut¹

1962

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II. The influence of temperature and adsorbed salts on the D.C. conductivity of polar polymer adsorbate systems

Cited by 26 publications

References 9 publications

A New Model of DC Conductivity of Hygroscopic Solids

A New Model of DC Conductivity of Hygroscopic Solids

Water structure-dependent charge transport in proteins.

The Dielectric Properties of Water and Their Role in Enzyme-Substrate Interactions

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