PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9217253-3 1997 To understand the mechanism that stabilizes the non-native intermediate, we characterized by circular dichroism (CD) the equilibrium unfolding transition of beta-lactoglobulin induced by guanidine hydrochloride (Gdn-HCl) at pH 2 and 4 degrees C. The unfolding transition measured by near-UV CD preceded the transition measured by far-UV CD, indicating the accumulation of the intermediate state. Guanidine 187-210 beta-lactoglobulin Bos taurus 157-175 9217253-3 1997 To understand the mechanism that stabilizes the non-native intermediate, we characterized by circular dichroism (CD) the equilibrium unfolding transition of beta-lactoglobulin induced by guanidine hydrochloride (Gdn-HCl) at pH 2 and 4 degrees C. The unfolding transition measured by near-UV CD preceded the transition measured by far-UV CD, indicating the accumulation of the intermediate state. Guanidine 212-219 beta-lactoglobulin Bos taurus 157-175 1368553-5 1990 The majority of the met-beta-lactoglobulin produced was found in an insoluble form but could be solubilized using guanidine-HCl. Guanidine 114-127 beta-lactoglobulin Bos taurus 24-42 8980687-1 1996 The kinetics of the guanidine hydrochloride-induced unfolding and refolding of bovine beta-lactoglobulin, a predominantly beta-sheet protein in the native state, have been studied by stopped-flow circular dichroism and absorption measurements at pH 3.2 and 4.5 degrees C. The refolding reaction was a complex process composed of different kinetic phases, while the unfolding was a single-phase reaction. Guanidine 20-43 beta-lactoglobulin Bos taurus 86-104 8980687-8 1996 (3) The circular dichroism spectra of beta-lactoglobulin and its disulfide-cleaved derivative in 4.0 M guanidine hydrochloride suggests the presence of the residual beta-structure in the unfolded state and the stabilization of the beta-structure by disulfide bonds. Guanidine 103-126 beta-lactoglobulin Bos taurus 38-56 8897609-1 1996 When bovine beta-lactoglobulin (beta-LG) was refolded after extensive denaturation in 4.8 M guanidine hydrochloride (GuHCl), the functional activity of the protein, retinol binding, as measured by the enhancement of this ligand"s fluorescence, was completely recovered. Guanidine 92-115 beta-lactoglobulin Bos taurus 12-30 8897609-1 1996 When bovine beta-lactoglobulin (beta-LG) was refolded after extensive denaturation in 4.8 M guanidine hydrochloride (GuHCl), the functional activity of the protein, retinol binding, as measured by the enhancement of this ligand"s fluorescence, was completely recovered. Guanidine 92-115 beta-lactoglobulin Bos taurus 32-39 8897609-1 1996 When bovine beta-lactoglobulin (beta-LG) was refolded after extensive denaturation in 4.8 M guanidine hydrochloride (GuHCl), the functional activity of the protein, retinol binding, as measured by the enhancement of this ligand"s fluorescence, was completely recovered. Guanidine 117-122 beta-lactoglobulin Bos taurus 12-30 8897609-1 1996 When bovine beta-lactoglobulin (beta-LG) was refolded after extensive denaturation in 4.8 M guanidine hydrochloride (GuHCl), the functional activity of the protein, retinol binding, as measured by the enhancement of this ligand"s fluorescence, was completely recovered. Guanidine 117-122 beta-lactoglobulin Bos taurus 32-39 7693669-3 1993 Bovine beta-lactoglobulin (beta-LG) was denatured in the presence of guanidine hydrochloride (GdnHCl) as the denaturant. Guanidine 69-92 beta-lactoglobulin Bos taurus 7-25 7693669-3 1993 Bovine beta-lactoglobulin (beta-LG) was denatured in the presence of guanidine hydrochloride (GdnHCl) as the denaturant. Guanidine 69-92 beta-lactoglobulin Bos taurus 27-34 7693669-3 1993 Bovine beta-lactoglobulin (beta-LG) was denatured in the presence of guanidine hydrochloride (GdnHCl) as the denaturant. Guanidine 94-100 beta-lactoglobulin Bos taurus 7-25 7693669-3 1993 Bovine beta-lactoglobulin (beta-LG) was denatured in the presence of guanidine hydrochloride (GdnHCl) as the denaturant. Guanidine 94-100 beta-lactoglobulin Bos taurus 27-34 7693669-4 1993 Renaturation of the denatured beta-LG was attempted by dialyzing to remove GdnHCl. Guanidine 75-81 beta-lactoglobulin Bos taurus 30-37 8043610-5 1994 A guanidine hydrochloride-induced unfolding study showed that the conformational stability of W19Y was greatly reduced by 6.9 kcal/mol compared to that of wild-type beta-LG. Guanidine 2-25 beta-lactoglobulin Bos taurus 165-172 29155106-2 2018 The present contribution elucidates the structural change of beta-lactoglobulin at pH7.4 under the action of guanidine hydrochloride (GnHCl) and heat at the single molecular level. Guanidine 109-132 beta-lactoglobulin Bos taurus 61-79 29155106-2 2018 The present contribution elucidates the structural change of beta-lactoglobulin at pH7.4 under the action of guanidine hydrochloride (GnHCl) and heat at the single molecular level. Guanidine 134-139 beta-lactoglobulin Bos taurus 61-79 16143573-1 2005 beta-Lactoglobulin (beta-LG) denatured with 6 M guanidine hydrochloride (GdnHCl) containing a reducing agent and subsequently dialysed against phosphate-buffered saline (PBS) resulted in incomplete refolding of this protein despite the fact that the biological activity for retinol-binding was recovered to almost the same degree as that of the native molecule [Hattori, M., Ametani, A., Katakura, Y., Shimizu, M., Kaminogawa, S. J., Biol. Guanidine 48-71 beta-lactoglobulin Bos taurus 0-18 18295961-3 2008 The guanidine hydrochloride (GuHCl)-induced unfolding transition and kinetic refolding of equine beta-lactoglobulin (ELG) by GuHCl-jump were investigated at pH 8.7 by far-ultraviolet circular dichroism. Guanidine 4-27 beta-lactoglobulin Bos taurus 97-115 18295961-3 2008 The guanidine hydrochloride (GuHCl)-induced unfolding transition and kinetic refolding of equine beta-lactoglobulin (ELG) by GuHCl-jump were investigated at pH 8.7 by far-ultraviolet circular dichroism. Guanidine 29-34 beta-lactoglobulin Bos taurus 97-115 18295961-3 2008 The guanidine hydrochloride (GuHCl)-induced unfolding transition and kinetic refolding of equine beta-lactoglobulin (ELG) by GuHCl-jump were investigated at pH 8.7 by far-ultraviolet circular dichroism. Guanidine 125-130 beta-lactoglobulin Bos taurus 97-115 16143573-1 2005 beta-Lactoglobulin (beta-LG) denatured with 6 M guanidine hydrochloride (GdnHCl) containing a reducing agent and subsequently dialysed against phosphate-buffered saline (PBS) resulted in incomplete refolding of this protein despite the fact that the biological activity for retinol-binding was recovered to almost the same degree as that of the native molecule [Hattori, M., Ametani, A., Katakura, Y., Shimizu, M., Kaminogawa, S. J., Biol. Guanidine 48-71 beta-lactoglobulin Bos taurus 20-27 16143573-1 2005 beta-Lactoglobulin (beta-LG) denatured with 6 M guanidine hydrochloride (GdnHCl) containing a reducing agent and subsequently dialysed against phosphate-buffered saline (PBS) resulted in incomplete refolding of this protein despite the fact that the biological activity for retinol-binding was recovered to almost the same degree as that of the native molecule [Hattori, M., Ametani, A., Katakura, Y., Shimizu, M., Kaminogawa, S. J., Biol. Guanidine 73-79 beta-lactoglobulin Bos taurus 0-18 16143573-1 2005 beta-Lactoglobulin (beta-LG) denatured with 6 M guanidine hydrochloride (GdnHCl) containing a reducing agent and subsequently dialysed against phosphate-buffered saline (PBS) resulted in incomplete refolding of this protein despite the fact that the biological activity for retinol-binding was recovered to almost the same degree as that of the native molecule [Hattori, M., Ametani, A., Katakura, Y., Shimizu, M., Kaminogawa, S. J., Biol. Guanidine 73-79 beta-lactoglobulin Bos taurus 20-27 15526300-1 2005 The chemical unfolding behavior of porcine beta-lactoglobulin (PLG) has been followed at pH 2 and 6 in the presence of guanidinium hydrochloride. Guanidine 119-144 beta-lactoglobulin Bos taurus 43-61