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Chemicals, plastics and rubber industries

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Capillary electrophoresis and dynamic light scattering studies of structure and binding characteristics of protein-polyelectrolyte complexes

Article Abstract:

Dynamic light scattering and capillary electrophoresis were used to analyze The complex formation between sodium polystyrenesulfonate and two proteins, bovine serum albumin and beta-lactoglobulin. It was observed that the conformations of these complexes are the same with those of protein-free polyelectrolyte. Moreover, the results conformed with a free-draining model for the complexes. The fitting parameters of the binding isotherms and the effect of the polyelectrolyte molecular weight on binding density show that the binding of beta-lactoglobulin is cooperative while the binding of bovine serum albumin is anticooperative.

Author: Dubin, Paul L., Gao, Jeff Y., Muhoberac, Barry B.
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
Polyelectrolytes

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Study of move set in cubic lattice model for protein folding

Article Abstract:

A study was conducted to analyze a move set in cubic lattice model for protein folding using Monte-Carlo simulations. Various combinations of trial probabilities for each move types were examined. The potential energy of a conformation was determined using the interaction energy parameter between monomers. Experimental results indicated that the Monte Carlo simulation of lattice folding correlated with the move set. In addition, a more flexible move set supported faster folding and higher foldicities.

Author: Shin, Jae-Min, Oh, Won Seok
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
Research, Usage, Protein folding, Lattice theory, Monte Carlo method, Monte Carlo methods

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Dispersion terms and analysis of size- and charge dependence in an enhanced poisson-boltzmann approach

Article Abstract:

A well-established concept to consider dispersion effects within a Poisson-Boltzmann approach of continuum solvation of proteins which could also be applied to study protein size or partial charge assignments is presented.

Author: Hansmann, Ulrich H.E., Kar, Parimal, Seel, Max, Hofinger, Siegfried
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2007
Continuum mechanics

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Subjects list: Analysis, Proteins
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