Beta-lactoglobulin: Difference between revisions
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<StructureSection load='1BEB' size=' | <StructureSection load='1BEB' size='350' 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]]. | |||
==3D structures of beta-lactoglobulin== | |||
[[Beta-lactoglobulin 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
__NOTOC__ | __NOTOC__ | ||
== | == References == | ||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 13:05, 14 April 2019
β-lactoglobulin [1] 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. 3D structures of beta-lactoglobulinBeta-lactoglobulin 3D structures
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ReferencesReferences
- ↑ 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