Molecular Playground/BLG: Difference between revisions
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β -lactoglobulin is a [[CBI Molecules]] being studied in the <span class="plainlinks">[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]</span> at UMass Amherst and on display at the <span class="plainlinks">[http://www.molecularplayground.org/ Molecular Playground]</span>. | β-lactoglobulin is a [[CBI Molecules]] being studied in the <span class="plainlinks">[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]</span> at UMass Amherst and on display at the <span class="plainlinks">[http://www.molecularplayground.org/ Molecular Playground]</span>. | ||
=== BLG as studied in the Dubin Lab === | === BLG as studied in the Dubin Lab === | ||
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. | |||
Revision as of 16:36, 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
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.