Main-chain Sorption of Water by Serum Albumin.

Brodersen, Rolf; Haugaard, B. J.; Jacobsen, C. F.; Pedersen, Anders Overgaard; Leander, Kurt; Swahn, Carl‐Gunnar

doi:10.3891/acta.chem.scand.27-0573

Cited by 10 publications

(1 citation statement)

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“…Even in the most recent literature, it is stated that this problem cannot be resolved by sorption-isotherm analysis However, there is a clear evidence from ir spectroscopy that the peptide backbone contains good hydration sites in a wide relative humidity range. [4][5][6][7] The aim of this work is to perform sorption experiments and at the same time to follow by ir spectroscopy the hydration of specific and representative sites of the protein such as the acidic side chains and the amide backbone carbonyls. Then using a model8 which postulates the existence of two main noninteracting classes of primary hydration sites and disregards the different binding free energy inside each class, the sorption isotherm of the ir irradiated sample can be decomposed and thermodynamic data concerning these strong and weak binding hydration sites can be obtained.…”

Section: Introductionmentioning

confidence: 99%

Lysozyme film hydration events: An IR and gravimetric study

Careri¹,

Giansanti²,

Gratton³

et al. 1979

Biopolymers

111

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By a combined gravimetric and ir technique, spectra of protein films are recorded during sorption isotherms at constant water content h (mg D2O/mg dry protein) in the range 0 les; h ⩽ 0.35 at 27 and 38°C. Computer-aided differential analysis shows the effect of progressive hydration on some significant sites of the protein such as the ionizable acidic side chains and the backbone amide carbonyls, as well as the spectrum of the adsorbed water itself. In order to derive thermodynamic properties of these sites, the measured sorption isotherm is decomposed in terms of a model which postulates the existence of two classes of primary sorption sites only, and these two contributions are independently checked by the ir data. The free energy of binding of the strong and weak binding sites is found to be 2.0 ± 0.2 and 0.40 ± 0.1 kcal/mol, respectively. A water-induced transition region is clearly detected in all the observed properties at 0.06 < h < 0.10 at 38°C and is shown to be due to changes involving both the structure of the absorbed water and the coverage of the absorption sites. A detailed picture of the hydration events is offered, and the relevance of these findings to protein dynamics is discussed

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Section: Introductionmentioning

confidence: 99%

Lysozyme film hydration events: An IR and gravimetric study

Careri¹,

Giansanti²,

Gratton³

et al. 1979

Biopolymers

111

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Thermodynamic functions of biopolymer hydration. I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process

Lüscher-Mattli

Rüegg

1982

Biopolymers

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SynopsisThe primary hydration process of native biopolymers is analyzed in a brief review of the literature, pertaining to various aspects of biopolymer-water systems. Based on this analysis, a hydration model is proposed that implies that the solution conformation of native biopolymers is stable at and above a critical degree of hydration (hp, = 0.060.1 g HzO/g polymer). This water content corresponds to the fraction of strongly bound water, and amounts to -20% of the primary hydration sphere. In order to test this model, detailed sorption-desorption scanning experiments were performed on a globular protein (a-chymotrypsin). The results obtained are consistent with the proposed hydration model. They show that under certain experimental conditions, sorption isotherms can be obtained that do not exhibit hysteresis. These data represent equilibrium conditions and are thus accessible to thermodynamic treatment. Valid thermodynamic functions, pertinent to the interaction of water with biopolymers in their solution state, can be obtained from these sorption experiments.

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The relationship of bound water to the IR amide I bandwidth of albumin

et al. 1986

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SynopsisFour different types of ir experiments, involving changes in pH, changes i n pressure, and the use of nonaqueous solvents, and with either albumin molecules dissolved in saline or adsorbed albumin films, support the hypothesis that the bandwidth of the amide I vibration of albumin is directly related to the amount of bound water in this protein. From the amide I band narrowing and the amide I shift to higher frequencies, it is proposed that a more ordered helix structure results as the amount of bound water is decreased.

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Main-chain Sorption of Water by Serum Albumin.

Cited by 10 publications

References 0 publications

Lysozyme film hydration events: An IR and gravimetric study

Lysozyme film hydration events: An IR and gravimetric study

Thermodynamic functions of biopolymer hydration. I. Their determination by vapor pressure studies, discussed in an analysis of the primary hydration process

The relationship of bound water to the IR amide I bandwidth of albumin

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