Interaction of dodecyl sulfate with native and modified .beta.-lactoglobulin

12‐Bromododecanoic acid binds inside the calyx of bovine β‐lactoglobulin

“…1). The extent of ligand‐protein interaction is consistent with the observed binding constants, K d , of ∼10 μM for this class of ligands [13–23].…”

“…For example, the structures of plasma retinol‐binding protein [6, 7]and epididymal retinoic acid binding protein [8]revealed buried retinoid species; the mouse major urinary protein a thiazoline derivative [9]; bilin‐binding protein a biliverdin molecule [10]; odorant‐binding protein an unidentified ligand, possibly a pyrazine derivative [11]; and for nitrophorin 1 a heme, bound through a histidine ligand to the protein [12]. There is evidence that bovine BLG binds a wide range of ligands, including fatty acids [13–23], retinol and retinol derivatives [20–27], porphyrin species [27, 28], assorted aromatic molecules [23, 29–32]and alkanone species [33, 34]. Despite many studies of ligand binding, there is, however, no unequivocal evidence as to where ligands, especially fatty‐acid type molecules, bind.…”

Cooperative α-helix formation of β-lactoglobulin induced by sodium n-alkyl sulfates

“…The interior of the β-barrel is hydrophobic, whereas the opening is lined with hydrophobic amino acids. The eight-stranded β-barrel is a major structural motif found in a family of proteins which have the ability to bind several amphiphilic or hydrophobic ligands [15,16] such as retinol [17], long-chain fatty [18] and sodium dodecyl sulfate [19][20][21][22].…”

Section C. Chemistry of milk proteins

“…On the other hand, all the other charged groups, except the extra histidine in /Mactoglobulin C, are accessible to H ions and may be assumed to lie on, or very near, the surface (36); also, the carboxyl end of the polypeptide chain is probably near or on the surface, since the terminal isoleucine and penultimate histidine are readily removed by carboxypeptidase without disruption of the rest of the molecule (112,177). Two of the 4 tyrosines can be acetylated without change of conformation, and though partly masked must lie close to the surface (471); one of the 2 tryptophans must also lie close to the surface (430).…”

“…Long-chain fatty acids are bound tightly (435), presumably at the same site as dodecyl sulphate, whose binding has been re-examined (284,388,430). The binding of such large anions as methyl orange (388), bromphenol blue (99) and JV-methyl-2anilino-6-naphthalene-sulphonate (284) has also been studied.…”