Molecular Playground/BLG: Difference between revisions
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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. | ||
=== BLG dimer turn === | |||
<scene name='Molecular_Playground/BLG/Blgscene/1'>BLG dimer</scene> | <scene name='Molecular_Playground/BLG/Blgscene/1'>BLG dimer</scene> | ||
Revision as of 16:43, 10 December 2010
β-lactoglobulin is a CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
BLG as studied in the Dubin LabBLG as studied in the Dubin Lab
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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).
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.
BLG dimer turnBLG dimer turn