This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Beta-lactoglobulin
From Proteopedia
| Line 1: | Line 1: | ||
| - | < | + | <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 === | ||
| - | |||
| - | <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). | '''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> | ||
| + | __NOTOC__ | ||
Revision as of 09:29, 28 August 2013
| |||||||||||
3D 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 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
