PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15624163-3 2005 We studied the effects of alkaline on two purified proteins, chicken insulin and bovine alpha-lactalbumin, both containing four disulfide bonds in their structure. Disulfides 128-137 lactalbumin alpha Bos taurus 88-105 17676769-0 2007 Heat treatment of bovine alpha-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity. Disulfides 72-81 lactalbumin alpha Bos taurus 25-42 15309367-7 2004 The percentage disulfide bond reduction increases as the urea concentration used for protein denaturation increases, giving a single-step sigmoid increment for single-domain, low-MW proteins (alpha-Lac and Lys), and a two-step sigmoid increment for multi-domain, high MW proteins (HSA and BSA). Disulfides 15-24 lactalbumin alpha Bos taurus 192-201 10076060-4 1999 Fragmentation of alpha-lactalbumin by chymotrypsin yielded CKDDQNPH ISCDKF (residues (61-68)S-S(75-80)), also a polypeptide composed of two polypeptide chains held together by a disulfide bridge. Disulfides 178-187 lactalbumin alpha Bos taurus 17-34 12369846-3 2002 S-(Carboxymethyl)-alpha-lactalbumin, a disordered form of the protein with three out of four disulfide bridges reduced, was even more susceptible to fibrillation. Disulfides 93-102 lactalbumin alpha Bos taurus 18-35 12081489-0 2002 Pathway of oxidative folding of alpha-lactalbumin: a model for illustrating the diversity of disulfide folding pathways. Disulfides 93-102 lactalbumin alpha Bos taurus 32-49 12081489-1 2002 The pathway of oxidative folding of alpha-lactalbumin (alpha LA) (four disulfide bonds) has been characterized by structural and kinetic analysis of the acid-trapped folding intermediates. Disulfides 71-80 lactalbumin alpha Bos taurus 36-53 10896943-2 2000 High affinity binding of Ca(2+) to alpha-lactalbumin (LA) stabilizes the native structure and is required for the efficient generation of native protein with correct disulfide bonds from the reduced denatured state. Disulfides 166-175 lactalbumin alpha Bos taurus 35-52 10896943-2 2000 High affinity binding of Ca(2+) to alpha-lactalbumin (LA) stabilizes the native structure and is required for the efficient generation of native protein with correct disulfide bonds from the reduced denatured state. Disulfides 166-175 lactalbumin alpha Bos taurus 54-56 11488928-8 2001 The two protein fragments of nicked or gapped alpha-LA are covalently linked by the four disulfide bridges of the native protein. Disulfides 89-98 lactalbumin alpha Bos taurus 46-54 11451435-1 2001 Fragment 53--103 of bovine alpha-lactalbumin, prepared by limited peptic digestion of the protein at low pH, is a 51-residue polypeptide chain crosslinked by two disulfide bonds encompassing helix C (residues 86--98) of the native protein. Disulfides 162-171 lactalbumin alpha Bos taurus 27-44 9250594-3 1997 Highly purified tryptic peptides from native and disulfide-bond-reduced alpha-La were obtained by reverse phase chromatography. Disulfides 49-58 lactalbumin alpha Bos taurus 72-80 10024465-11 1999 The absorption of 250-nm light by disulfide bonds also provided information regarding the proper folding of rat prolactin and bovine alpha-lactalbumin. Disulfides 34-43 lactalbumin alpha Bos taurus 133-150 10024465-9 1999 Bovine alpha-lactalbumin, 14 kDa with four disulfide bonds, required complete renaturation prior to the removal of a reducing agent. Disulfides 43-52 lactalbumin alpha Bos taurus 7-24 9685721-4 1998 The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin. Disulfides 35-44 lactalbumin alpha Bos taurus 53-70 9685721-4 1998 The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin. Disulfides 35-44 lactalbumin alpha Bos taurus 160-177 9685721-4 1998 The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin. Disulfides 143-152 lactalbumin alpha Bos taurus 53-70 9685721-4 1998 The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin. Disulfides 143-152 lactalbumin alpha Bos taurus 160-177 9685721-6 1998 The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL. Disulfides 10-19 lactalbumin alpha Bos taurus 54-71 9685721-6 1998 The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL. Disulfides 36-45 lactalbumin alpha Bos taurus 54-71 9685721-6 1998 The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL. Disulfides 36-45 lactalbumin alpha Bos taurus 171-188 9685721-6 1998 The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL. Disulfides 36-45 lactalbumin alpha Bos taurus 54-71 9685721-6 1998 The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL. Disulfides 36-45 lactalbumin alpha Bos taurus 171-188 8732764-1 1996 alpha-Lactalbumin is a small, globular protein that is stabilized by four disulfide bonds and contains two structural domains. Disulfides 74-83 lactalbumin alpha Bos taurus 0-17 8732764-5 1996 The three-disulfide form, having a reduced Cys 6-Cys 120 disulfide bond with carboxymethylated cysteines, is similar to intact alpha-lactalbumin in secondary and tertiary structure as judged by its ellipticity in the near and far UV. Disulfides 10-19 lactalbumin alpha Bos taurus 127-144 8732764-6 1996 the two-disulfide form of alpha-lactalbumin, having reduced Cys 6-Cys 120 and Cys 28-Cys 111 disulfide bonds with carboxymethylated cysteines, retains about half the secondary and tertiary structure of the intact alpha-lactalbumin. Disulfides 8-17 lactalbumin alpha Bos taurus 26-43 8732764-6 1996 the two-disulfide form of alpha-lactalbumin, having reduced Cys 6-Cys 120 and Cys 28-Cys 111 disulfide bonds with carboxymethylated cysteines, retains about half the secondary and tertiary structure of the intact alpha-lactalbumin. Disulfides 8-17 lactalbumin alpha Bos taurus 213-230 8732764-8 1996 We conclude that, in the two disulfide form, alpha-lactalbumin retains its calcium-binding beta-domain, whereas the alpha-domain is unfolded. Disulfides 29-38 lactalbumin alpha Bos taurus 45-62 8466909-7 1993 The native structure of alpha-lactalbumin appears to be split by selective disulfide bond cleavage into at least one subdomain, which retains the Ca(2+)-binding site. Disulfides 75-84 lactalbumin alpha Bos taurus 24-41 7513556-3 1994 The present study investigates the effect of DsbA on the well-characterized disulfide-coupled refolding processes of BPTI and of alpha-lactalbumin. Disulfides 76-85 lactalbumin alpha Bos taurus 129-146 7513556-6 1994 Neither did DsbA catalyze the intramolecular rearrangements observed in the three disulfide-bonded "molten globule" form of alpha-lactalbumin at neutral pH. Disulfides 82-91 lactalbumin alpha Bos taurus 124-141 8747428-0 1995 Conformational changes of alpha-lactalbumin induced by the stepwise reduction of its disulfide bridges: the effect of the disulfide bridges on the structural stability of the protein in sodium dodecyl sulfate solution. Disulfides 85-94 lactalbumin alpha Bos taurus 26-43 8747428-0 1995 Conformational changes of alpha-lactalbumin induced by the stepwise reduction of its disulfide bridges: the effect of the disulfide bridges on the structural stability of the protein in sodium dodecyl sulfate solution. Disulfides 122-131 lactalbumin alpha Bos taurus 26-43 8747428-1 1995 Four disulfide bridges of bovine alpha-lactalbumin (alpha-lact) were selectively reduced to obtain its derivatives with three, two, and zero disulfide bridges (designated as 3SS, 2SS, and 0SS alpha-lact, respectively). Disulfides 5-14 lactalbumin alpha Bos taurus 33-50 8747434-0 1995 The superreactive disulfide bonds in alpha-lactalbumin and lysozyme. Disulfides 18-27 lactalbumin alpha Bos taurus 37-54 8747434-2 1995 The local conformation around the surface disulfide in ELZ seems to be more similar to that in hen egg-white lysozyme than in alpha-lactalbumin. Disulfides 42-51 lactalbumin alpha Bos taurus 126-143 8747434-4 1995 The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond. Disulfides 34-44 lactalbumin alpha Bos taurus 54-71 8747434-4 1995 The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond. Disulfides 34-44 lactalbumin alpha Bos taurus 285-302 8747434-4 1995 The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond. Disulfides 34-43 lactalbumin alpha Bos taurus 54-71 8747434-4 1995 The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond. Disulfides 34-43 lactalbumin alpha Bos taurus 285-302 8466908-0 1993 Pathway of disulfide-coupled unfolding and refolding of bovine alpha-lactalbumin. Disulfides 11-20 lactalbumin alpha Bos taurus 63-80 8466908-1 1993 alpha-Lactalbumin"s four disulfide bonds have been used to probe the nature of its native, molten globule, and unfolded states. Disulfides 25-34 lactalbumin alpha Bos taurus 0-17 8466909-0 1993 Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin. Disulfides 35-44 lactalbumin alpha Bos taurus 77-94 8466909-1 1993 Specific three- and two-disulfide intermediates that accumulate transiently during reduction of the disulfide bonds of Ca(2+)-bound bovine alpha-lactalbumin have been trapped, isolated, and characterized. Disulfides 24-33 lactalbumin alpha Bos taurus 139-156 8466909-1 1993 Specific three- and two-disulfide intermediates that accumulate transiently during reduction of the disulfide bonds of Ca(2+)-bound bovine alpha-lactalbumin have been trapped, isolated, and characterized. Disulfides 100-109 lactalbumin alpha Bos taurus 139-156 8466909-4 1993 The remaining native disulfide bonds in the two partially reduced derivatives of alpha-lactalbumin are stable only when the proteins are in a Ca(2+)-bound state. Disulfides 21-30 lactalbumin alpha Bos taurus 81-98 35111980-0 2022 Sensitive and resistant of the homologous disulfide-bridged proteins alpha-lactalbumin and lysozyme to attack of hydrogen-atoms, dithiothreitol and trifluoroacetic acid, examined by matrix-assisted laser desorption/ionization mass spectrometry. Disulfides 42-51 lactalbumin alpha Bos taurus 69-86 28926961-1 2017 Bovine alpha-lactalbumin (alphaLA) has four disulfide (SS) bonds in the native form (N). Disulfides 44-53 lactalbumin alpha Bos taurus 7-24 23296632-1 2013 Upon controlled UV illumination, disulfide bonds in bovine alpha-lactalbumin (BLA) are selectively broken, leading to self-assembly of the BLA and doxorubicin (DOX) molecules into nanoparticles via hydrophobic interactions and intermolecular disulfide bonds. Disulfides 33-42 lactalbumin alpha Bos taurus 59-76 23296632-1 2013 Upon controlled UV illumination, disulfide bonds in bovine alpha-lactalbumin (BLA) are selectively broken, leading to self-assembly of the BLA and doxorubicin (DOX) molecules into nanoparticles via hydrophobic interactions and intermolecular disulfide bonds. Disulfides 242-251 lactalbumin alpha Bos taurus 59-76 22189830-0 2012 Characterization of an alternative low energy fold for bovine alpha-lactalbumin formed by disulfide bond shuffling. Disulfides 90-99 lactalbumin alpha Bos taurus 62-79 22189830-1 2012 Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA. Disulfides 53-62 lactalbumin alpha Bos taurus 7-24 22189830-1 2012 Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA. Disulfides 53-62 lactalbumin alpha Bos taurus 26-33 22189830-1 2012 Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA. Disulfides 53-62 lactalbumin alpha Bos taurus 87-94 22189830-2 2012 This X-alphaLA isomer contains two native disulfide bridges (Cys 6-Cys 120 and Cys 28-Cys 111) and two non-native disulfide bridges (Cys 61-Cys 73 and Cys 77-Cys 91). Disulfides 42-51 lactalbumin alpha Bos taurus 7-14 22189830-2 2012 This X-alphaLA isomer contains two native disulfide bridges (Cys 6-Cys 120 and Cys 28-Cys 111) and two non-native disulfide bridges (Cys 61-Cys 73 and Cys 77-Cys 91). Disulfides 114-123 lactalbumin alpha Bos taurus 7-14 22189830-3 2012 MD simulations have been used to characterize the X-alphaLA isomer and its formation via disulfide bond shuffling and to compare it with the native fold of alphaLA. Disulfides 89-98 lactalbumin alpha Bos taurus 52-59 22189830-8 2012 Calcium binding to native alphaLA is shown to help preserve the structure of the beta-domain of the protein limiting possibilities for disulfide bond shuffling. Disulfides 135-144 lactalbumin alpha Bos taurus 26-33 18942855-0 2008 Disulfide bond shuffling in bovine alpha-lactalbumin: MD simulation confirms experiment. Disulfides 0-9 lactalbumin alpha Bos taurus 35-52 2783142-0 1989 Calcium regulates folding and disulfide-bond formation in alpha-lactalbumin. Disulfides 30-39 lactalbumin alpha Bos taurus 58-75 2783142-1 1989 Refolding and disulfide bond formation in reduced denatured bovine alpha-lactalbumin is shown to be Ca2+-dependent. Disulfides 14-23 lactalbumin alpha Bos taurus 67-84 6871261-9 1983 It is concluded that in Ca2+-saturated alpha-lactalbumin some tryptophane residues are located near the quenching groups (dynamic quenching), most likely the disulfide bridges. Disulfides 158-167 lactalbumin alpha Bos taurus 39-56 5532232-0 1970 The disulfide bonds of bovine alpha-lactalbumin. Disulfides 4-13 lactalbumin alpha Bos taurus 30-47 27273301-1 2016 Bovine alpha-lactalbumin (alpha-La) is a major food allergen found in milk and is characterized by high conformational stability because of its four disulfide bridges and being calcium bound. Disulfides 149-158 lactalbumin alpha Bos taurus 7-24 27273301-1 2016 Bovine alpha-lactalbumin (alpha-La) is a major food allergen found in milk and is characterized by high conformational stability because of its four disulfide bridges and being calcium bound. Disulfides 149-158 lactalbumin alpha Bos taurus 26-34 32481977-5 2013 The disulfide bonds in protein bovine alpha-lactalbumin (BLA) can be ruptured by controlled UV illumination, which triggers the formation of nano-sized protein aggregates and releases free thiol groups for the modification of the active targeting ligand of circular RGD peptide. Disulfides 4-13 lactalbumin alpha Bos taurus 38-55