Electric Polarization in Proteins—Dielectric Dispersion and Kerr Effect Studies of Isoionic Bovine Serum Albumin<sup>1</sup>

Moser, P.; Squire, Phil G.; O’Konski, Chester T.

doi:10.1021/j100875a023

Cited by 96 publications

(67 citation statements)

References 5 publications

(7 reference statements)

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“…The harmonic mean of the rotational diffusion correlation time of the macromolecule was calculated on the basis of this triaxial ellipsoid to be 49.5 ns. This value is in conformity with the 47.6-54.9ns measured with fluorescence depolarization and dielectric relaxation experiments (Moser, Squire & O'Konski, 1966;Wahl, 1966;Steiner, 1953). The prediction algorithm has been discussed recently (Miiller, 1991).…”

Section: Determination Of the Lee From Experimentalsupporting

confidence: 87%

The inertia-equivalent ellipsoid: a link between atomic structure and low-resolution models of small globular proteins determined by small-angle X-ray scattering

Müller¹,

Schrauber²

1992

J Appl Cryst

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Low‐resolution three‐parameter models of the shape of a biopolymer in solution can be determined by a new indirect method from small‐angle X‐ray scattering without contrast‐variation experiments. The basic low‐resolution model employed is a triaxial ellipsoid – the inertia‐equivalent ellipsoid (IEE). The IEE is related to the tensor of inertia of a body and the eigenvalues and eigenvectors of this tensor can be calculated directly from the atomic coordinates and from the homogeneous solvent‐excluded body of a molecule. The IEE defines a mean molecular surface (like the sea level on earth) which models the molecular shape adequately if the IEE volume is not more than 30% larger than the dry volume of the molecule. Approximately 10 to 15% of the solvent‐excluded volume is outside the ellipsoid; the radii of gyration of the IEE and of the homogeneous molecular body are identical. The largest diameter of the IEE is about 5 to 15% (~0.2–0.8 nm) smaller than the maximum dimension of globular molecules with molecular masses smaller than 65000 daltons. From the scattering curve of a molecule in solution the IEE can be determined by a calibration procedure. 29 proteins of known crystal structure have been used as a random sample. Systematic differences between the axes of the IEE, calculated directly from the structure, and the axes of the scattering‐equivalent ellipsoids of revolution, estimated from the scattering curve of the molecule in solution, are used to derive correction factors for the axial dimensions. Distortions of model dimensions of 20 to 40% (up to 1 nm), caused by misinterpretation of scattering contributions from electron density fluctuations within the molecule, are reduced to a quarter by applying these correction factors to the axes of the scattering‐equivalent ellipsoids of revolution. In a computer experiment the axes of the inertia‐equivalent ellipsoids have been determined for a further nine proteins with the same accuracy. The automated estimation of the IEE from the scattering curve of a molecule in solution is realized by the Fortran77 program AUTOIEE.

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Section: Determination Of the Lee From Experimentalsupporting

confidence: 87%

The inertia-equivalent ellipsoid: a link between atomic structure and low-resolution models of small globular proteins determined by small-angle X-ray scattering

Müller¹,

Schrauber²

1992

J Appl Cryst

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“…The rotational reorientation of the BSA molecule is anisotropic, with correlation times in the range of 25-100 ns (20,21). When the shortest correlation time (25 ns) and the theoretical analysis for isotropic reorientation are used, the predicted vi, of a methylene or methyl resonance is .100 Hz and the predicted NOE is the minimum value of 1.15 (22).…”

Section: Aqueousmentioning

confidence: 99%

Interactions of myristic acid with bovine serum albumin: a 13C NMR study.

Hamilton¹,

Cistola²,

Morrisett³

et al. 1984

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

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Interactions of myristic acid with bovine serum albumin were studied by 13C NMR spectroscoy at 50.3 MHz using 90% isotopically substituted [1-'3C1-, [3-C] 13C]myristic acid to bovine serum albumin (from 0.7 to 5.6) revealed at least two narrow resonances for each carbon at all molar ratios. Thus, bovine serum albumin binding sites for myristic acid are heterogeneous with respect to titration behavior and with respect to the local magnetic environment at both the polar and the nonpolar ends of the fatty acid. The narrow resonances observed for the methylene and methyl carbons are inconsistent with complete immobilization of the protein-bound acid molecules. Together with spin-lattice relaxation times and nuclear Overhauser enhancements, the linewidth results indicate that bound myristic acid has internal motions that are rapid compared with overall protein tumbling and that the C-3 methylene carbon is more restricted than the terminal methyl carbon.

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“…Globular proteins have the unusually large dipole moments, in comparison with the dipole moment of water molecules (1.84 D) (Antosiewicz 1995). For example, the dipole moment of HSA and BSA is equal to 700 D and 384 D, respectively (Moser et al 1966). The values of the activation energy of HSA (∆E p = 8.77 × 10 5 kJ/mol) and BSA (∆E p = 5.96 × 10 5 kJ/mol) obtained in solutions at pI show that the higher value of the dipole moment the higher value of the activation energy of albumin.…”

Section: Resultsmentioning

confidence: 99%

A viscometric approach of pH effect on hydrodynamic properties of human serum albumin in the normal form

Monkos¹

2013

gpb

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Abstract. The paper presents the results of viscosity determinations on aqueous solutions of human serum albumin (HSA) at isoelectric point over a wide range of concentrations and at temperatures ranging from 5°C to 45°C. On the basis of a modified Arrhenius equation and Mooney's formula some hydrodynamic parameters were obtained. They are compared with those previously obtained for HSA in solutions at neutral pH. The activation energy and entropy of viscous flow and the intrinsic viscosity reach a maximum value, and the effective specific volume, the self-crowding factor and the Huggins coefficient a minimum value in solutions at isoelectric point. Using the dimensionless parameter [η]c, the existence of three ranges of concentrations: diluted, semi-diluted and concentrated, was shown. By applying Lefebvre's relation for the relative viscosity in the semi-dilute regime, the Mark-Houvink-Kuhn-Sakurada (MHKS) exponent was established. The analysis of the results obtained from the three ranges of concentrations showed that both conformation and stiffness of HSA molecules in solutions at isoelectric point and at neutral pH are the same.

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Electric Polarization in Proteins—Dielectric Dispersion and Kerr Effect Studies of Isoionic Bovine Serum Albumin¹

Cited by 96 publications

References 5 publications

The inertia-equivalent ellipsoid: a link between atomic structure and low-resolution models of small globular proteins determined by small-angle X-ray scattering

The inertia-equivalent ellipsoid: a link between atomic structure and low-resolution models of small globular proteins determined by small-angle X-ray scattering

Interactions of myristic acid with bovine serum albumin: a 13C NMR study.

A viscometric approach of pH effect on hydrodynamic properties of human serum albumin in the normal form

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Electric Polarization in Proteins—Dielectric Dispersion and Kerr Effect Studies of Isoionic Bovine Serum Albumin1

Cited by 96 publications

References 5 publications

The inertia-equivalent ellipsoid: a link between atomic structure and low-resolution models of small globular proteins determined by small-angle X-ray scattering

The inertia-equivalent ellipsoid: a link between atomic structure and low-resolution models of small globular proteins determined by small-angle X-ray scattering

Interactions of myristic acid with bovine serum albumin: a 13C NMR study.

A viscometric approach of pH effect on hydrodynamic properties of human serum albumin in the normal form

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Product

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Electric Polarization in Proteins—Dielectric Dispersion and Kerr Effect Studies of Isoionic Bovine Serum Albumin¹

A viscometric approach of pH effect on hydrodynamic properties of human serum albumin in the normal form