Beta-lactoglobulin: Difference between revisions

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'''β-lactoglobulin''' is a dimeric protein that exists in two forms.  BLG A and BLG B, which differ by two mutations, one of which is a non-charged residue being replaced by an Aspartic Acid, which at relevant pH values is negatively charged.  The result is a protein that exists in two isoforms, which differ by two negative charges (one per monomer).
'''β-lactoglobulin''' is a dimeric protein that exists in two forms.  BLG A and BLG B, which differ by two mutations, one of which is a non-charged residue being replaced by an Aspartic Acid, which at relevant pH values is negatively charged.  The result is a protein that exists in two isoforms, which differ by two negative charges (one per monomer).


The differences between these two forms significantly augment the electrostatic potential, making BLG A & BLG B an ideal system for studying the interaction of a protein with a polyelectrolyte.
The differences between these two forms significantly augment the electrostatic potential, making BLG A & BLG B an ideal system for studying the interaction of a protein with a polyelectrolyte.  More details in [[Molecular Playground/BLG]].


    
    

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Michal Harel, Alexander Berchansky