PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14040204-0 1961 Reaction of reduced disulfide bonds in alpha-lactalbumin and beta-lactoglobulin with acrylonitrile. Disulfides 20-29 lactalbumin alpha Homo sapiens 39-56 2753599-0 1989 Contribution of disulfide bonds to stability of the folding intermediate of alpha-lactalbumin. Disulfides 16-25 lactalbumin alpha Homo sapiens 76-93 2753599-1 1989 The secondary structure formed in disulfide reduced alpha-lactalbumin is investigated by CD spectrum and is compared with that of the folding intermediate of the disulfide intact protein. Disulfides 34-43 lactalbumin alpha Homo sapiens 52-69 22044-2 1977 Behavior of sulfhydryl and disulfide groups in alkali-treated beta-lactoglobulin and alpha-lactalbumin]. Disulfides 27-36 lactalbumin alpha Homo sapiens 85-102 29096436-8 2017 Cross-linking was associated with formation of sulfenic acids (RS-OH species), oxidation of methionine residues, cleavage of disulfide bonds in alpha-lactalbumin, altered conformation of disulfide bonds in beta-lactoglobulin, alterations in the fluorescence intensity and maximum emission wavelength of endogenous tryptophan residues, and binding of the hydrophobic probe 8-anilinonaphthalenesulfonate. Disulfides 125-134 lactalbumin alpha Homo sapiens 144-161 27393305-5 2016 Here, we directly imaged GroEL-GroES interaction in the presence of disulfide-reduced alpha-lactalbumin as a substrate protein using high-speed atomic force microscopy. Disulfides 68-77 lactalbumin alpha Homo sapiens 86-103 28351690-6 2017 The apo form of alpha-lactalbumin (aLA) forms liprotides at room temperature, however, Ovalbumin (Ova) and Bovine Serum Albumin (BSA) require elevated temperatures (>=60 C) to form liprotides, and in addition, they need to be returned to lower temperatures to remain stable; repeated cycles of heating and cooling gradually dissociate the liprotides in parallel with the formation of disulfide-bonded aggregates. Disulfides 387-396 lactalbumin alpha Homo sapiens 16-33 26304368-6 2016 The alpha-La:beta-lactoglobulin (beta-Lg) ratio greatly affected the nature of the interactions formed during gelation, where higher amounts of alpha-La lead to a gel more dependent on disulfide bonds. Disulfides 185-194 lactalbumin alpha Homo sapiens 4-12 26304368-6 2016 The alpha-La:beta-lactoglobulin (beta-Lg) ratio greatly affected the nature of the interactions formed during gelation, where higher amounts of alpha-La lead to a gel more dependent on disulfide bonds. Disulfides 185-194 lactalbumin alpha Homo sapiens 144-152 22899503-5 2012 In contrast, although the milk protein alpha-lactalbumin has several disulfide bridges, only one phenylarsenic moiety was bound under strongly denaturing conditions. Disulfides 69-78 lactalbumin alpha Homo sapiens 39-56 24077854-8 2013 By adjusting the settings, the EC reaction efficiency was gradually changed from partial to full disulfide bonds reduction in alpha-lactalbumin, and the expected shift in charge state distribution has been demonstrated. Disulfides 97-106 lactalbumin alpha Homo sapiens 126-143 22417479-6 2011 Our results also suggested that the formation of intermolecular disulfide bonds together with noncovalent interactions are the main mechanisms resulting in the moisture-induced aggregation of alpha-lactalbumin in model systems. Disulfides 64-73 lactalbumin alpha Homo sapiens 192-209 22201548-10 2012 The thermal stability of alpha-La stabilized emulsions in the presence of salt is a combined effect of the electrostatic repulsion and the lack of covalent disulfide interchange reactions. Disulfides 156-165 lactalbumin alpha Homo sapiens 25-33 21197958-7 2011 Furthermore, electrolytic reduction of proteins (e.g., alpha-lactalbumin) leads to increased charges on the detected protein ions, revealing the role of disulfide bonds on maintaining protein conformation. Disulfides 153-162 lactalbumin alpha Homo sapiens 55-72 15050830-1 2004 NMR spectroscopy has been used to follow the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each with a single proline substitution in a helix. Disulfides 116-125 lactalbumin alpha Homo sapiens 143-160 19152385-0 2009 Protein instability during HIC: evidence of unfolding reversibility, and apparent adsorption strength of disulfide bond-reduced alpha-lactalbumin variants. Disulfides 105-114 lactalbumin alpha Homo sapiens 128-145 19152385-4 2009 Additionally, variants of alpha-lactalbumin in which one of the disulfide bonds is reduced were synthesized to examine the effects of conformational stability on apparent retention. Disulfides 64-73 lactalbumin alpha Homo sapiens 26-43 16302782-5 2005 It seemed likely that, at 800 MPa, the formation of a beta-LG disulfide-bonded network preceded the formation of disulfide bonds between alpha-LA or BSA and beta-LG to form multiprotein aggregates, possibly because the disulfide bonds of alpha-LA and BSA are less exposed than those of beta-LG either during or after pressure treatment. Disulfides 62-71 lactalbumin alpha Homo sapiens 137-145 16302782-5 2005 It seemed likely that, at 800 MPa, the formation of a beta-LG disulfide-bonded network preceded the formation of disulfide bonds between alpha-LA or BSA and beta-LG to form multiprotein aggregates, possibly because the disulfide bonds of alpha-LA and BSA are less exposed than those of beta-LG either during or after pressure treatment. Disulfides 113-122 lactalbumin alpha Homo sapiens 137-145 16302782-5 2005 It seemed likely that, at 800 MPa, the formation of a beta-LG disulfide-bonded network preceded the formation of disulfide bonds between alpha-LA or BSA and beta-LG to form multiprotein aggregates, possibly because the disulfide bonds of alpha-LA and BSA are less exposed than those of beta-LG either during or after pressure treatment. Disulfides 113-122 lactalbumin alpha Homo sapiens 137-145 15545361-4 2004 These results indicate that beta-LG and alpha-LA associated with MFGM proteins via disulfide bonds during the high-pressure treatment of whole milk. Disulfides 83-92 lactalbumin alpha Homo sapiens 40-48 20557125-3 2010 As corroborated by electrophoresis analysis, both beta-lactoglobulin (beta-lg) and alpha-lactalbumin (alpha-la) were involved in the formation of aggregates via the thiol-disulfide interchange reaction and/or noncovalent interactions. Disulfides 171-180 lactalbumin alpha Homo sapiens 83-100 15050830-2 2004 [28-111] alpha-LA forms a molten globule very similar to that formed by the wild-type four-disulfide protein, and this variant has been used as a model for the alpha-lactalbumin (alpha-LA) molten globule in a number of studies. Disulfides 91-100 lactalbumin alpha Homo sapiens 9-17 12784209-6 2003 Mass spectrometry data obtained for trypsin-fragmented UV-illuminated alpha-lactalbumin with acrylodan-modified free thiol groups reveal the reduction of the 61-77 and 73-91 disulfide bridges. Disulfides 174-183 lactalbumin alpha Homo sapiens 70-87 15115177-0 2004 Two-state folding of lysozyme versus multiple-state folding of alpha-lactalbumin illustrated by the technique of disulfide scrambling. Disulfides 113-122 lactalbumin alpha Homo sapiens 63-80 12784209-0 2003 Ultraviolet illumination-induced reduction of alpha-lactalbumin disulfide bridges. Disulfides 64-73 lactalbumin alpha Homo sapiens 46-63 14690403-0 2003 Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin. Disulfides 25-34 lactalbumin alpha Homo sapiens 120-137 14690403-1 2003 Intermolecular disulfide bond formation in pure beta-lactoglobulin (beta-Lg) B and in its 1:1 mixture with alpha-lactalbumin (alpha-La), heated at 85 degrees C for 10 min in solutions of low and high (100 mM NaCl) ionic strength and pH 6.0, was studied by reverse-phase HPLC and MALDI-TOF mass spectrometry. Disulfides 15-24 lactalbumin alpha Homo sapiens 107-124 14690403-1 2003 Intermolecular disulfide bond formation in pure beta-lactoglobulin (beta-Lg) B and in its 1:1 mixture with alpha-lactalbumin (alpha-La), heated at 85 degrees C for 10 min in solutions of low and high (100 mM NaCl) ionic strength and pH 6.0, was studied by reverse-phase HPLC and MALDI-TOF mass spectrometry. Disulfides 15-24 lactalbumin alpha Homo sapiens 126-134 12603172-5 2003 High charge states of both cytochrome c and disulfide-reduced alpha-lactalbumin homodimers dissociate by a symmetrical charge partitioning process in which both fragment monomers carry away roughly an equal number of charges. Disulfides 44-53 lactalbumin alpha Homo sapiens 62-79 11560938-0 2002 The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling. Disulfides 72-81 lactalbumin alpha Homo sapiens 23-40 11560938-3 2002 Under strong denaturing conditions (e.g. 6 m guanidinium chloride) and in the presence of a thiol initiator, alpha-lactalbumin (alphaLA) denatures by shuffling its four native disulfide bonds and converts to an assembly of 45 species of scrambled isomers. Disulfides 176-185 lactalbumin alpha Homo sapiens 109-126 10756101-2 2000 Here, we used circular dichroism and disulfide exchange experiments to examine the unfolding mechanism of alpha-LA(alpha), a two- disulfide variant of human alpha-lactalbumin (alpha-LA) that adopts a molten globule conformation under near physiological conditions. Disulfides 37-46 lactalbumin alpha Homo sapiens 106-114 11518539-1 2001 The hydrogen-exchange behavior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has been examined and compared with that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants of [28-111] alpha-lactalbumin. Disulfides 108-118 lactalbumin alpha Homo sapiens 69-86 11518539-1 2001 The hydrogen-exchange behavior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has been examined and compared with that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants of [28-111] alpha-lactalbumin. Disulfides 108-117 lactalbumin alpha Homo sapiens 69-86 11118458-0 2001 The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin. Disulfides 76-85 lactalbumin alpha Homo sapiens 27-44 11118458-1 2001 The structure of denatured alpha-lactalbumin (alpha-LA) has been characterized using the method of disulfide scrambling. Disulfides 99-108 lactalbumin alpha Homo sapiens 27-44 11118458-1 2001 The structure of denatured alpha-lactalbumin (alpha-LA) has been characterized using the method of disulfide scrambling. Disulfides 99-108 lactalbumin alpha Homo sapiens 46-54 11118458-2 2001 Under denaturing conditions (urea, guanidine hydrochloride, guanidine thiocyanate, organic solvent or elevated temperature) and in the presence of thiol initiator, alpha-LA denatures by shuffling its four native disulfide bonds and converts to a mixture of fully oxidized scrambled structures. Disulfides 212-221 lactalbumin alpha Homo sapiens 164-172 11266594-3 2001 To explore the nature of side-chain--side-chain interactions in the alpha-lactalbumin (alpha-LA) molten globule, we determined the effective concentration for formation of the 28--111 disulfide bond in 14 double-mutant proteins, each containing two hydrophobic core residues replaced by alanine. Disulfides 184-193 lactalbumin alpha Homo sapiens 87-95 11150528-1 2000 A predominant conformational isomer of non-native alpha-lactalbumin (alpha-LA) has been purified by thermal denaturation of the native alpha-LA using the technique of disulfide scrambling. Disulfides 167-176 lactalbumin alpha Homo sapiens 50-67 11150528-1 2000 A predominant conformational isomer of non-native alpha-lactalbumin (alpha-LA) has been purified by thermal denaturation of the native alpha-LA using the technique of disulfide scrambling. Disulfides 167-176 lactalbumin alpha Homo sapiens 69-77 10820057-4 2000 When 10% solutions of 1:1 (w/w) mixtures of alpha-La and BSA were heated, large disulfide-bonded aggregates and SDS-monomeric BSA and alpha-La were present. Disulfides 80-89 lactalbumin alpha Homo sapiens 44-52 10820057-6 2000 These results suggest that BSA forms disulfide-bonded aggregates that contain available thiol groups that can catalyze the formation of differently structured alpha-La monomers, dimers, higher polymers, and adducts of alpha-La with BSA. Disulfides 37-46 lactalbumin alpha Homo sapiens 159-167 11718563-7 2001 In contrast to the isolated alpha-helical domain of alpha-lactalbumin, Lyso-alpha with two native disulfide bonds exhibits a well-defined tertiary structure, as indicated by cooperative thermal unfolding and a well-dispersed NMR spectrum. Disulfides 98-107 lactalbumin alpha Homo sapiens 52-69 11368628-6 2001 The results also indicated that the aggregates and intermediates, which contained dimeric and trimeric alpha-La, were mainly formed by the intermolecular disulfide bonds. Disulfides 154-163 lactalbumin alpha Homo sapiens 103-111 10820057-6 2000 These results suggest that BSA forms disulfide-bonded aggregates that contain available thiol groups that can catalyze the formation of differently structured alpha-La monomers, dimers, higher polymers, and adducts of alpha-La with BSA. Disulfides 37-46 lactalbumin alpha Homo sapiens 218-226 10756101-2 2000 Here, we used circular dichroism and disulfide exchange experiments to examine the unfolding mechanism of alpha-LA(alpha), a two- disulfide variant of human alpha-lactalbumin (alpha-LA) that adopts a molten globule conformation under near physiological conditions. Disulfides 130-139 lactalbumin alpha Homo sapiens 106-114 9684889-0 1998 Transition state in the folding of alpha-lactalbumin probed by the 6-120 disulfide bond. Disulfides 73-82 lactalbumin alpha Homo sapiens 35-52 10623614-1 2000 The binding processes of GroEL with apo cytochrome c (apo-cyt c) and disulfide-reduced apo alpha-lactalbumin (rLA) in homogeneous solution at low concentration were analyzed by fluorescence correlation spectroscopy (FCS) with extremely high sensitivity. Disulfides 69-78 lactalbumin alpha Homo sapiens 91-108 10606762-0 2000 Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state. Disulfides 45-54 lactalbumin alpha Homo sapiens 63-80 10606762-2 2000 A set of peptides has been prepared in order to probe the role of local interactions in the vicinity of the Cys(6)-Cys(120) disulfide bond in stabilizing the molten globule state of human alpha-lactalbumin. Disulfides 124-133 lactalbumin alpha Homo sapiens 188-205 10694412-3 2000 SecB binds both fully unfolded RNase A and BPTI as well as compact, partially folded disulfide intermediates of alpha-lactalbumin, which have 40-60% of native secondary structure. Disulfides 85-94 lactalbumin alpha Homo sapiens 112-129 10504730-1 1999 Human alpha-lactalbumin (alpha-LA) is a four disulfide-bonded protein that adopts partially structured conformations under a variety of mildly denaturing conditions. Disulfides 45-54 lactalbumin alpha Homo sapiens 6-23 10504730-1 1999 Human alpha-lactalbumin (alpha-LA) is a four disulfide-bonded protein that adopts partially structured conformations under a variety of mildly denaturing conditions. Disulfides 45-54 lactalbumin alpha Homo sapiens 25-33 10504730-8 1999 These results show that the overall architecture of the protein fold of alpha-LA is determined by the polypeptide sequence itself, and not as the result of cross-linking by disulfide bonds, and provide insight into the way in which the sequence codes for the fold. Disulfides 173-182 lactalbumin alpha Homo sapiens 72-80 10500168-0 1999 The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding. Disulfides 11-20 lactalbumin alpha Homo sapiens 41-58 10500168-1 1999 Our aim is to determine whether the disulfide bonds of alpha-lactalbumin account for the lack of cooperative folding behavior reported for some molten globule variants, in contrast to the highly cooperative folding reported for the pH 4 molten globule of apomyoglobin. Disulfides 36-45 lactalbumin alpha Homo sapiens 55-72 9653039-4 1998 In order to understand the mechanism for formation of the native-like tertiary topology, we substituted alanine for each of the 23 buried residues in the alpha-helical domain of alpha-LA and determined the effect of these substitutions on the Ceff for formation of the 28-111 disulfide bond. Disulfides 276-285 lactalbumin alpha Homo sapiens 178-186 9684889-1 1998 The guanidine hydrochloride concentration dependence of the folding and unfolding rate constants of a derivative of alpha-lactalbumin, in which the 6-120 disulfide bond is selectively reduced and S-carboxymethylated, was measured and compared with that of disulfide-intact alpha-lactalbumin. Disulfides 154-163 lactalbumin alpha Homo sapiens 116-133 9684889-1 1998 The guanidine hydrochloride concentration dependence of the folding and unfolding rate constants of a derivative of alpha-lactalbumin, in which the 6-120 disulfide bond is selectively reduced and S-carboxymethylated, was measured and compared with that of disulfide-intact alpha-lactalbumin. Disulfides 256-265 lactalbumin alpha Homo sapiens 116-133 8547266-0 1996 Disulfide determinants of calcium-induced packing in alpha-lactalbumin. Disulfides 0-9 lactalbumin alpha Homo sapiens 53-70 9133623-1 1997 alpha-Lactalbumin in which all the disulfide bonds are fully reduced (RLA) is known to bind strongly to the chaperonin GroEL. Disulfides 35-44 lactalbumin alpha Homo sapiens 0-17 8895096-10 1996 The oligomers of alpha-lactalbumin are stabilized mainly by nonnative interchain disulfide bridges. Disulfides 81-90 lactalbumin alpha Homo sapiens 17-34 8637013-3 1996 The binding constant was estimated to be in the order of 10(5) M-1 by analyzing the kinetic data quantitatively and was found to be much weaker than the binding between GroEL and disulfide-bond reduced alpha-lactalbumin, whose binding constant is in the order of 10(7) M-1. Disulfides 179-188 lactalbumin alpha Homo sapiens 202-219 8547266-4 1996 alpha-LA(alpha) contains only the two disulfide bonds in the alpha-helical domain of alpha-LA, while alpha-LA(beta) contains only the beta-sheet domain and interdomain disulfide bonds. Disulfides 38-47 lactalbumin alpha Homo sapiens 0-8 8547266-4 1996 alpha-LA(alpha) contains only the two disulfide bonds in the alpha-helical domain of alpha-LA, while alpha-LA(beta) contains only the beta-sheet domain and interdomain disulfide bonds. Disulfides 38-47 lactalbumin alpha Homo sapiens 85-93 8547266-4 1996 alpha-LA(alpha) contains only the two disulfide bonds in the alpha-helical domain of alpha-LA, while alpha-LA(beta) contains only the beta-sheet domain and interdomain disulfide bonds. Disulfides 38-47 lactalbumin alpha Homo sapiens 85-93 8547266-7 1996 Thus, specific interactions within alpha-LA imposed by the beta-sheet domain and interdomain disulfide bonds, as opposed to the two alpha-helical domain disulfides, are necessary for the calcium-induced progression from the molten globule toward more native-like structure. Disulfides 93-102 lactalbumin alpha Homo sapiens 35-43 7880819-7 1995 Our results suggest that molten globules contain regions with varying degrees of specificity for native-like structure and that the core region surrounding the 28-111 disulfide bond plays an important role in alpha-LA folding by stabilizing the molten globule intermediate. Disulfides 167-176 lactalbumin alpha Homo sapiens 209-217 8011632-2 1994 RNase T1 and alpha-lactalbumin were reduced and converted to mixed disulfide derivatives, named GS-RNase T1 and GS-alpha-lactalbumin, in good yield; the molecular masses of the derivatives were confirmed by electrospray mass spectrometry. Disulfides 67-76 lactalbumin alpha Homo sapiens 13-30 7986345-2 1994 Secondary structural changes of the cleaved alpha-lactalbumin, in which the two separated polypeptides were joined by disulfide bridges, were examined in solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride. Disulfides 118-127 lactalbumin alpha Homo sapiens 44-61 8312273-0 1994 Disulfide-rearranged molten globule state of alpha-lactalbumin. Disulfides 0-9 lactalbumin alpha Homo sapiens 45-62 1472507-0 1992 Contribution of the 6-120 disulfide bond of alpha-lactalbumin to the stabilities of its native and molten globule states. Disulfides 26-35 lactalbumin alpha Homo sapiens 44-61 1472507-1 1992 The unfolding and refolding of a derivative of alpha-lactalbumin, in which the disulfide bond between Cys6 and Cys120 is selectively reduced and S-carboxymethylated, are investigated by equilibrium and kinetic circular dichroism measurements. Disulfides 79-88 lactalbumin alpha Homo sapiens 47-64 34359447-1 2021 UV-B illumination facilitates aggregation of alpha-lactalbumin (alpha-LA) by intramolecular disulfide bond cleavage followed by intermolecular thiol-disulfide exchange reactions. Disulfides 92-101 lactalbumin alpha Homo sapiens 45-62 34359447-1 2021 UV-B illumination facilitates aggregation of alpha-lactalbumin (alpha-LA) by intramolecular disulfide bond cleavage followed by intermolecular thiol-disulfide exchange reactions. Disulfides 149-158 lactalbumin alpha Homo sapiens 45-62 35236515-4 2022 This behavior was ascribed to the fact that alpha-lactalbumin (alpha-La) and beta-lactoglobulin (beta-Lg) contained in WPI denatured after heating and engaged in disulfide bond formation with each other. Disulfides 162-171 lactalbumin alpha Homo sapiens 44-61