Molecular Playground/BLG: Difference between revisions

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=== BLG as studied in the Dubin Lab ===
=== BLG as studied in the Dubin Lab ===


<Structure load='1BEB' size='500' frame='true' align='right' caption='BLG A and BLG B are isoforms that differ by 2 charge units' scene='Molecular_Playground/BLG/Blgscene/1' />
<Structure load='1BEB' size='400' frame='true' align='right' caption='BLG A and BLG B are isoforms that differ by 2 charge units [[1beb]]' scene='Molecular_Playground/BLG/Blgscene/1' />


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.

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Daniel Seeman, Michal Harel, Alexander Berchansky