Beta-lactoglobulin: Difference between revisions
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< | <StructureSection load='1BEB' size='450' side='right' scene='Molecular_Playground/BLG/Blgscene/1' caption=''> | ||
'''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>. | ||
{{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> | |||
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Revision as of 12:29, 28 August 2013
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 Labβ-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. |
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3D structures of beta-lactoglobulin3D structures of beta-lactoglobulin
Updated on 28-August-2013
1beb, 1bsy, 2blg, 3blg, 1dv9, 1qg5, 1b8e, 2akq, 2q2m, 2q2p, 2q39, 3npo, 3ph5, 3ph6 – bBlac – bovine
1bsq, 1cj5, 1uz2 – bBlac (mutant)
3kza – bBlac/hBlac - horse
1exs – Blac – pig
1yup – Blac – reindeer
Beta-lactoglobulin complexesBeta-lactoglobulin complexes
1b0o, 3uew – bBlac + palmitate
1bso – bBlac + bromododecanoic acid
3nq3, 3nq9, 3qzj, 3qzk, 3uex – bBlac + fatty acid
3ueu - bBlac + lauric acid
3uev - bBlac + myristic acid
1gx9 – bBlac + retinoic acid
1gxa - bBlac + retinoic acid + palmitate
2gj5 – bBlac + vitamin D3
2r56 – bBlac + antibody