PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6526379-9 1984 We found that the free thiol group, localized at position 121 or in equal amounts at positions 119 and 121 in bovine beta-lactoglobulin, is absent in beta-lactoglobulin I from horse colostrum. Sulfhydryl Compounds 23-28 beta-lactoglobulin Bos taurus 117-135 6526379-9 1984 We found that the free thiol group, localized at position 121 or in equal amounts at positions 119 and 121 in bovine beta-lactoglobulin, is absent in beta-lactoglobulin I from horse colostrum. Sulfhydryl Compounds 23-28 beta-lactoglobulin Bos taurus 150-168 31087497-1 2019 Bovine beta-lactoglobulin (BLG) is a major whey protein with unique structural characteristics: it possesses a free Cys thiol (SH) and two disulfide (SS) bonds and consists of a beta-barrel core surrounded by one long and several short alpha helices. Sulfhydryl Compounds 120-125 beta-lactoglobulin Bos taurus 7-25 31087497-1 2019 Bovine beta-lactoglobulin (BLG) is a major whey protein with unique structural characteristics: it possesses a free Cys thiol (SH) and two disulfide (SS) bonds and consists of a beta-barrel core surrounded by one long and several short alpha helices. Sulfhydryl Compounds 120-125 beta-lactoglobulin Bos taurus 27-30 31087497-9 2019 These findings are informative not only for elucidating oxidative folding pathways of other members of the beta-lactoglobulin family, but also for understanding the roles of a redundant Cys thiol in the oxidative folding process of a protein with odd Cys residues. Sulfhydryl Compounds 190-195 beta-lactoglobulin Bos taurus 107-125 26041244-5 2015 It was shown that the conformational changes of beta-LG after conjugation with GF3 were bigger than that with GF4, including quenching of fluorescence intensity, the red-shift of fluorescence spectra, and the increase in sulfhydryl content. Sulfhydryl Compounds 221-231 beta-lactoglobulin Bos taurus 48-55 12963719-8 2003 Kinetics of the formation of the irreversibly unfolded species of wild-type beta-lg in 8 M urea at pH 7.0 indicated that, first, an intramolecular thiol-disulfide exchange occurs to produce a mixture of species with non-native disulfide bonds followed by the intermolecular thiol-disulfide exchange producing the oligomers. Sulfhydryl Compounds 274-279 beta-lactoglobulin Bos taurus 76-83 19330636-8 2009 Upon heating beta-Lg at neutral pH, native dimer starts to dissociate into monomers leading to the exposure of previously buried hydrophobic amino acids and the free thiol group. Sulfhydryl Compounds 166-171 beta-lactoglobulin Bos taurus 13-20 18662787-3 2008 This free thiol group has been shown to be responsible for the irreversibility of BLG denaturation in vitro, but nothing is known about its relevance during protein folding inside the cell. Sulfhydryl Compounds 10-15 beta-lactoglobulin Bos taurus 82-85 17235131-6 2007 Cross-linking the free thiol groups of beta-LG by heating (100 degrees C for 2 min), or chemically modifying the beta-LG by carboxymethylation to block the thiol groups resulted in a substantial loss of antioxidant activity. Sulfhydryl Compounds 23-28 beta-lactoglobulin Bos taurus 39-46 17235131-6 2007 Cross-linking the free thiol groups of beta-LG by heating (100 degrees C for 2 min), or chemically modifying the beta-LG by carboxymethylation to block the thiol groups resulted in a substantial loss of antioxidant activity. Sulfhydryl Compounds 156-161 beta-lactoglobulin Bos taurus 39-46 16554059-0 2006 Comparison of the conformational stability of the non-native alpha-helical intermediate of thiol-modified beta-lactoglobulin upon interaction with sodium n-alkyl sulfates at two different pH. Sulfhydryl Compounds 91-96 beta-lactoglobulin Bos taurus 106-124 16554059-2 2006 beta-lactoglobulin has a free thiol at Cys121, which is buried between the beta-barrel and the C-terminal major or alpha-helix. Sulfhydryl Compounds 30-35 beta-lactoglobulin Bos taurus 0-18 16554059-3 2006 This thiol group was specifically reacted with DTNB (5,5"-dithiobis(2-nitrobenzoic acid)) at pH 7.5 and 2, producing a modified beta-lactoglobulin containing a mix disulfide bond with 5-thio-2-nitrobenzoic acid (TNB). Sulfhydryl Compounds 5-10 beta-lactoglobulin Bos taurus 128-146 16554059-5 2006 The formation of non-native alpha-helical intermediate of thiol modified beta-lactoglobulin (TNB-beta-LG) was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; sodium dodecyl sulfate, SDS; and sodium tetradecyl sulfate, STS at pH 7.5 and 2. Sulfhydryl Compounds 58-63 beta-lactoglobulin Bos taurus 73-91 16554059-5 2006 The formation of non-native alpha-helical intermediate of thiol modified beta-lactoglobulin (TNB-beta-LG) was induced by n-alkyl sulfates including sodium octyl sulfate, SOS; sodium decyl sulfate, SDeS; sodium dodecyl sulfate, SDS; and sodium tetradecyl sulfate, STS at pH 7.5 and 2. Sulfhydryl Compounds 58-63 beta-lactoglobulin Bos taurus 97-104 16190664-1 2005 Bovine beta-lactoglobulin B (beta-LG) is susceptible to pressure treatment, which unfolds it, allowing thiol-catalyzed disulfide bond interchange to occur, facilitating intermolecular bonding (both noncovalent and disulfide). Sulfhydryl Compounds 103-108 beta-lactoglobulin Bos taurus 7-27 16190664-1 2005 Bovine beta-lactoglobulin B (beta-LG) is susceptible to pressure treatment, which unfolds it, allowing thiol-catalyzed disulfide bond interchange to occur, facilitating intermolecular bonding (both noncovalent and disulfide). Sulfhydryl Compounds 103-108 beta-lactoglobulin Bos taurus 29-36 15605716-4 2004 Addition of a sulphydryl-oxidising agent, KlO3, to milk or whey increased HP-induced denaturation of beta-lg, but reduced the denaturation of alpha-la. Sulfhydryl Compounds 14-24 beta-lactoglobulin Bos taurus 101-108 15605716-5 2004 Denaturation of both alpha-la and beta-lg was prevented by adding a sulphydryl-blocking agent, N-ethylmaleimide, to milk or whey prior to HP treatment, highlighting the crucial role of sulphydryl-disulphide interchange reactions in HP-induced denaturation of alpha-la and beta-lg. Sulfhydryl Compounds 68-78 beta-lactoglobulin Bos taurus 34-41 15147215-3 2004 This free thiol plays an important role in the heat-induced aggregation of BLG and, possibly, in its conformational stability. Sulfhydryl Compounds 10-15 beta-lactoglobulin Bos taurus 75-78 12963719-8 2003 Kinetics of the formation of the irreversibly unfolded species of wild-type beta-lg in 8 M urea at pH 7.0 indicated that, first, an intramolecular thiol-disulfide exchange occurs to produce a mixture of species with non-native disulfide bonds followed by the intermolecular thiol-disulfide exchange producing the oligomers. Sulfhydryl Compounds 147-152 beta-lactoglobulin Bos taurus 76-83 12963719-9 2003 These results indicate that intramolecular and intermolecular thiol-disulfide exchange reactions cause the low reversibility of wild-type beta-lg especially at neutral pH and that the mutation of Cys-121 improves the reversibility, enabling us to study the folding of beta-lg more exactly under various conditions. Sulfhydryl Compounds 62-67 beta-lactoglobulin Bos taurus 138-145 19362581-2 2009 However, compared to other textbook proteins, progress in the study of beta LG has been slow because of obstacles such as a low reversibility from denaturation linked with thiol-disulfide exchange or monomer-dimer equilibrium preventing a detailed NMR analysis. Sulfhydryl Compounds 172-177 beta-lactoglobulin Bos taurus 71-78 19281275-4 2009 In contrast, the activities of the whey proteins were dependent on denaturation or partial hydrolysis and dominated by the free thiol in beta-lg. Sulfhydryl Compounds 128-133 beta-lactoglobulin Bos taurus 137-144 18465840-2 2008 In the mutant, a free thiol group of wild-type beta-lg at Cys121 was removed and two beta-lg molecules were linked by a disulfide bridge through Cys34 created at the dimer"s interface. Sulfhydryl Compounds 22-27 beta-lactoglobulin Bos taurus 47-54 17235131-6 2007 Cross-linking the free thiol groups of beta-LG by heating (100 degrees C for 2 min), or chemically modifying the beta-LG by carboxymethylation to block the thiol groups resulted in a substantial loss of antioxidant activity. Sulfhydryl Compounds 156-161 beta-lactoglobulin Bos taurus 113-120 16368109-1 2006 The Tanford transition is a conformational change of bovine beta-lactoglobulin (betaLG) occurring at around pH 7, identified originally on the basis of optical rotatory dispersion and the accessibility of a thiol group. Sulfhydryl Compounds 207-212 beta-lactoglobulin Bos taurus 60-78 11694050-8 2001 These results are consistent with a mechanism in which the free thiols of heat-treated beta-lg or BSA catalyse the formation of a range of monomers, dimers and higher polymers of alpha-la. Sulfhydryl Compounds 64-70 beta-lactoglobulin Bos taurus 87-94 11045618-0 2000 Conformation and stability of thiol-modified bovine beta-lactoglobulin. Sulfhydryl Compounds 30-35 beta-lactoglobulin Bos taurus 52-70 11045618-2 2000 Beta-lactoglobulin A has a free thiol at Cys121, which is buried between the beta-barrel and the C-terminal major alpha-helix. Sulfhydryl Compounds 32-37 beta-lactoglobulin Bos taurus 0-18 11045618-3 2000 This thiol group was specifically reacted with 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) in the presence of 1.0 M Gdn-HCI at pH 7.5, producing a modified beta-lactoglobulin (TNB-bIg) containing a mixed disulfide bond with 5-thio-2-nitrobenzoic acid (TNB). Sulfhydryl Compounds 5-10 beta-lactoglobulin Bos taurus 155-173 10563854-4 1999 These changes resulted in a specific denatured beta-LG monomer, which covalently associated via the free thiol group. Sulfhydryl Compounds 105-110 beta-lactoglobulin Bos taurus 47-54 9876928-8 1998 Computer analysis of possible interactions involving Cys121 in a three-dimensional structure of beta-lactoglobulin revealed that the thiol group is too far away from neighboring residues to form side-chain hydrogen bonds. Sulfhydryl Compounds 133-138 beta-lactoglobulin Bos taurus 96-114 18634071-1 1997 The major component of the whey fraction of bovine milk, beta-lactoglobulin (betaLG), has been transformed by grafting polyethylene glycol chains either on the thiol group (free and after reduction of the S-S bridges) of the cysteine residues, or on the amino group of the lysine residues and/or of the N-terminal amino acid. Sulfhydryl Compounds 160-165 beta-lactoglobulin Bos taurus 57-75