1bsy

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsy OCA], [https://pdbe.org/1bsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bsy RCSB], [https://www.ebi.ac.uk/pdbsum/1bsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bsy ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN]] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.

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== Publication Abstract from PubMed ==

The structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition.

Structural basis of the Tanford transition of bovine beta-lactoglobulin.,Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB Biochemistry. 1998 Oct 6;37(40):14014-23. PMID:9760236<ref>PMID:9760236</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1bsy" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Baker, E N]]

[[Category: Bewley, M C]]

[[Category: Creamer, L K]]

[[Category: Jameson, G B]]

[[Category: Qin, B Y]]

[[Category: Transport]]