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Beta-lactoglobulin

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<Structure load='1b0o' size='400' frame='true' align='right' caption=' Bovine beta-lactoglobulin complex with palmitate [[1b0o]]' scene= />
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<StructureSection load='1BEB' size='350' side='right' scene='Molecular_Playground/BLG/Blgscene/1' caption='Bovine β-lactoglobulin (PDB code [[1beb]])'>
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'''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>.
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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>.
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{{Clear}}
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=== BLG as studied in the Dubin Lab ===
=== BLG as studied in the Dubin Lab ===
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<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' />
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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).
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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. More details in [[Molecular Playground/BLG]].
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==3D structures of beta-lactoglobulin==
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[[Beta-lactoglobulin 3D structures]]
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</StructureSection>
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__NOTOC__
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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).
 
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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.
 
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'''Beta-lactoglobulin''' details in [[Molecular Playground/BLG]].
 
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==3D structures of beta-lactoglobulin==
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== References ==
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<references/>
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[[1beb]], [[1bsy]], [[2blg]], [[3blg]], [[1dv9]], [[1qg5]], [[1b8e]], [[2akq]], [[2q2m]], [[2q2p]], [[2q39]], [[3npo]], [[3ph5]], [[3ph6]] – bBlac – bovine<br />
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[[1bsq]], [[1cj5]], [[1uz2]] – bBlac (mutant) <br />
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[[3kza]] – bBlac/hBlac - horse<br />
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[[1exs]] – Blac – pig<br />
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[[1yup]] – Blac – reindeer
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===Beta-lactoglobulin complexes===
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[[1b0o]], [[3uew]] – bBlac + palmitate<br />
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[[1bso]] – bBlac + bromododecanoic acid<br />
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[[3nq3]], [[3nq9]], [[3qzj]], [[3qzk]], [[3uex]] – bBlac + fatty acid<br />
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[[3ueu]] - bBlac + lauric acid<br />
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[[3uev]] - bBlac + myristic acid<br />
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[[1gx9]] – bBlac + retinoic acid<br />
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[[1gxa]] - bBlac + retinoic acid + palmitate<br />
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[[2gj5]] – bBlac + vitamin D3<br />
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[[2r56]] – bBlac + antibody
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[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Bovine β-lactoglobulin (PDB code 1beb)

Drag the structure with the mouse to rotate


References

  1. ↑ Kontopidis G, Holt C, Sawyer L. Invited review: beta-lactoglobulin: binding properties, structure, and function. J Dairy Sci. 2004 Apr;87(4):785-96. PMID:15259212 doi:http://dx.doi.org/10.3168/jds.S0022-0302(04)73222-1

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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