Electrophoresis of protein charge ladders: a comparison of experiment with various continuum primitive models
Article Abstract:
The free solution electrophoretic mobilities of the charge ladders of five proteins are modeled within the framework of the continuum primitive model. The model can yield mobilities in excellent agreement with experiment provided the underlying models are realistic representations of the actual solution structure. The model provides a useful approach for determining the values of DeltaZ, the change in net charge of proteins due to chemical modification of charged groups.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2004
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Effects of cooperativity in proton binding on the net charge of proteins in charge ladders
Article Abstract:
The effects of cooperativity of proton binding on values of net charge and the change in net charge of a protein deltaZ due to the modification of charged groups is reported. The capillary electrophoresis (CE) and charge ladders are used to measure the net charge of lysozyme and values of pK(Sub a) of the N-terminal alpha-amino group of this protein with different numbers of Lys epsilon-amino groups acetylated.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2003
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Simulation and modeling of the Rhodobacter sphaeroides bacterial reaction center: Structure and interactions
Article Abstract:
A molecular dynamics (MD) simulation of a reaction center (RC) protein of Rhodobacter sphaeroides is reported in a water and detergent solution. The latter component, (Lauryl Dimethyl Amino Oxide) LDAO a nonionic amphile, is used to protect the transmembrane helices of three RC and provides a micelle-like structure to cover the RC hydrophobic regions.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2003
User Contributions:
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