Molecular Playground/BLG: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Daniel Seeman, Michal Harel, Alexander Berchansky

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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 ===
-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).
+<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).
+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.