Beta-lactoglobulin: Difference between revisions

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<StructureSection load='1BEB' size='450' side='right' scene='Molecular_Playground/BLG/Blgscene/1' caption='Bovine β-lactoglobulin (PDB code [[1beb]])'>
<StructureSection load='1BEB' size='450' side='right' scene='Molecular_Playground/BLG/Blgscene/1' caption='Bovine β-lactoglobulin (PDB code [[1beb]])'>
'''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''' <ref>PMID:15259212</ref> 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>.
{{Clear}}
{{Clear}}
=== 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. More details in [[Molecular Playground/BLG]].
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]].
</StructureSection>
</StructureSection>
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**[[2r56]] – bBlac + antibody
**[[2r56]] – bBlac + antibody
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== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

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

Michal Harel, Alexander Berchansky