PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24750237-4 2014 BPTI has several features in common with a subset of antimicrobial proteins in that it is small, cationic and stabilized by disulphide bonds. disulphide 124-134 spleen trypsin inhibitor I Bos taurus 0-4 10080904-0 1999 Stability of the residual structure in unfolded BPTI in different conditions of temperature and solvent composition measured by disulphide kinetics and double mutant cycle analysis. disulphide 128-138 spleen trypsin inhibitor I Bos taurus 48-52 9450353-5 1998 The results show that the disulphide bonds of BPTI contribute to the folding of the gas phase ions, but that even in the absence of disulphide bonds the protein ions maintain compact structures. disulphide 26-36 spleen trypsin inhibitor I Bos taurus 46-50 9450353-6 1998 Comparisons to relative areas calculated from hydrodynamic radii of BPTI in solution suggest that when disulphide linkages are removed, BPTI in the gas phase unfolds less than BPTI in solution. disulphide 103-113 spleen trypsin inhibitor I Bos taurus 68-72 9450353-6 1998 Comparisons to relative areas calculated from hydrodynamic radii of BPTI in solution suggest that when disulphide linkages are removed, BPTI in the gas phase unfolds less than BPTI in solution. disulphide 103-113 spleen trypsin inhibitor I Bos taurus 136-140 9450353-6 1998 Comparisons to relative areas calculated from hydrodynamic radii of BPTI in solution suggest that when disulphide linkages are removed, BPTI in the gas phase unfolds less than BPTI in solution. disulphide 103-113 spleen trypsin inhibitor I Bos taurus 136-140 8632454-1 1996 The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI) revealed that the native conformation is still stable in each intermediate state with two native disulphide linkages, in the absence of each of the corresponding third disulphide bonds. disulphide 4-14 spleen trypsin inhibitor I Bos taurus 71-75 8632454-1 1996 The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI) revealed that the native conformation is still stable in each intermediate state with two native disulphide linkages, in the absence of each of the corresponding third disulphide bonds. disulphide 174-184 spleen trypsin inhibitor I Bos taurus 71-75 8632454-1 1996 The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI) revealed that the native conformation is still stable in each intermediate state with two native disulphide linkages, in the absence of each of the corresponding third disulphide bonds. disulphide 174-184 spleen trypsin inhibitor I Bos taurus 71-75 8632454-5 1996 The conformation of a chemically trapped two-disulphide intermediate in the disulphide refolding of dendrotoxin K, with blocking groups on Cys5 and Cys55 and disulphide bonds between Cys30 and Cys51, and Cys14 and Cys38, respectively, has been determined by 1H NMR spectroscopy and compared to those of the native protein and of the corresponding intermediate in BPTI. disulphide 45-55 spleen trypsin inhibitor I Bos taurus 363-367 8632454-5 1996 The conformation of a chemically trapped two-disulphide intermediate in the disulphide refolding of dendrotoxin K, with blocking groups on Cys5 and Cys55 and disulphide bonds between Cys30 and Cys51, and Cys14 and Cys38, respectively, has been determined by 1H NMR spectroscopy and compared to those of the native protein and of the corresponding intermediate in BPTI. disulphide 76-86 spleen trypsin inhibitor I Bos taurus 363-367 8632454-7 1996 It is similar to the partly-folded conformation of the BPTI intermediate with just the Cys30-Cys-51 disulphide bond, but with a more fixed conformation in the region of the Cys14-Cys38 disulphide bond. disulphide 100-110 spleen trypsin inhibitor I Bos taurus 55-59 8632454-7 1996 It is similar to the partly-folded conformation of the BPTI intermediate with just the Cys30-Cys-51 disulphide bond, but with a more fixed conformation in the region of the Cys14-Cys38 disulphide bond. disulphide 185-195 spleen trypsin inhibitor I Bos taurus 55-59 1960731-1 1991 An analogue of the BPTI folding intermediate that contains only the disulphide bonds between Cys14 and Cys38 and between Cys30 and Cys51 has been prepared in Escherichia coli by protein engineering methods. disulphide 68-78 spleen trypsin inhibitor I Bos taurus 19-23 8846225-1 1995 Bovine pancreatic trypsin inhibitor (BPTI) does not fold by simple sequential formation of its native disulphide bonds. disulphide 102-112 spleen trypsin inhibitor I Bos taurus 0-35 8846225-1 1995 Bovine pancreatic trypsin inhibitor (BPTI) does not fold by simple sequential formation of its native disulphide bonds. disulphide 102-112 spleen trypsin inhibitor I Bos taurus 37-41 8846225-5 1995 The need to unfold previously acquired native structure, observed in the folding of BPTI, may be a common feature of disulphide-linked folding reactions. disulphide 117-127 spleen trypsin inhibitor I Bos taurus 84-88 7552729-4 1995 Although the other native one-disulphide intermediates, [30-51] and [5-55], are thermodynamically more stable, [14-38] can be populated substantially at the early stages of BPTI folding. disulphide 30-40 spleen trypsin inhibitor I Bos taurus 173-177 7540214-1 1995 The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI), especially at the two-disulphide stage, has been dissected by replacing one or two particular cysteine residues by serine. disulphide 4-14 spleen trypsin inhibitor I Bos taurus 71-75 7540214-1 1995 The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI), especially at the two-disulphide stage, has been dissected by replacing one or two particular cysteine residues by serine. disulphide 100-110 spleen trypsin inhibitor I Bos taurus 71-75 7540214-3 1995 The results obtained confirm the kinetic roles in the original BPTI pathway of the two specific two-disulphide intermediates with non-native second disulphide bonds, (30-51, 5-14) and (30-51, 5-38). disulphide 100-110 spleen trypsin inhibitor I Bos taurus 63-67 7540214-3 1995 The results obtained confirm the kinetic roles in the original BPTI pathway of the two specific two-disulphide intermediates with non-native second disulphide bonds, (30-51, 5-14) and (30-51, 5-38). disulphide 148-158 spleen trypsin inhibitor I Bos taurus 63-67 7504737-5 1993 The roles of these interactions in folding of reduced BPTI could be determined, as the conformational and nuclear magnetic resonance properties of all the major disulphide intermediates are known. disulphide 161-171 spleen trypsin inhibitor I Bos taurus 54-58 7694758-13 1993 The region containing two of the disulphide bonds (around Cys5-Cys55 and Cys30-Cys51) and much of the secondary structure is essential for the binding affinity of the toxins, while the region around Cys14 and Cys38, equivalent to part of the antiprotease site of the homologous protease inhibitor from bovine pancreas (BPTI), plays an important role in the potency of dendrotoxins. disulphide 33-43 spleen trypsin inhibitor I Bos taurus 319-323 7507172-1 1994 The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. disulphide 80-90 spleen trypsin inhibitor I Bos taurus 129-133 7507172-1 1994 The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. disulphide 158-168 spleen trypsin inhibitor I Bos taurus 129-133 7690463-6 1993 Here we report that PDI increases by a factor of 3,000-6,000 the rates of folding of kinetically trapped BPTI folding intermediates, in which native structure impedes disulphide bond formation. disulphide 167-177 spleen trypsin inhibitor I Bos taurus 105-109 7689114-2 1993 The kinetics of disulphide bond formation and breakage have been measured in five analogues of the single-disulphide intermediates that occur in folding of bovine pancreatic trypsin inhibitor (BPTI), in which the cysteine residues not involved in disulphide bonds have been replaced by serine residues. disulphide 16-26 spleen trypsin inhibitor I Bos taurus 193-197 7689114-2 1993 The kinetics of disulphide bond formation and breakage have been measured in five analogues of the single-disulphide intermediates that occur in folding of bovine pancreatic trypsin inhibitor (BPTI), in which the cysteine residues not involved in disulphide bonds have been replaced by serine residues. disulphide 106-116 spleen trypsin inhibitor I Bos taurus 193-197 7689114-2 1993 The kinetics of disulphide bond formation and breakage have been measured in five analogues of the single-disulphide intermediates that occur in folding of bovine pancreatic trypsin inhibitor (BPTI), in which the cysteine residues not involved in disulphide bonds have been replaced by serine residues. disulphide 106-116 spleen trypsin inhibitor I Bos taurus 193-197 7689114-5 1993 The intramolecular rate of forming each disulphide bond was found in the dithiol forms of reduced BPTI to be approximately proportional inversely to the size of the disulphide loop formed. disulphide 40-50 spleen trypsin inhibitor I Bos taurus 98-102 7689114-5 1993 The intramolecular rate of forming each disulphide bond was found in the dithiol forms of reduced BPTI to be approximately proportional inversely to the size of the disulphide loop formed. disulphide 165-175 spleen trypsin inhibitor I Bos taurus 98-102 7680380-2 1993 An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. disulphide 72-82 spleen trypsin inhibitor I Bos taurus 53-57 1373775-1 1992 The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. disulphide 111-121 spleen trypsin inhibitor I Bos taurus 47-82 1373775-1 1992 The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. disulphide 111-121 spleen trypsin inhibitor I Bos taurus 84-88 1373775-1 1992 The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. disulphide 280-290 spleen trypsin inhibitor I Bos taurus 47-82 1373775-1 1992 The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. disulphide 280-290 spleen trypsin inhibitor I Bos taurus 84-88 1960732-0 1991 Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. disulphide 73-83 spleen trypsin inhibitor I Bos taurus 108-143 1960732-1 1991 An analogue of the bovine pancreatic trypsin inhibitor (BPTI) folding intermediate that contains only the disulphide bond between Cys5 and Cys55 has been prepared in Escherichia coli by protein engineering methods, with the other four Cys residues replaced by Ser. disulphide 106-116 spleen trypsin inhibitor I Bos taurus 19-54 1960732-1 1991 An analogue of the bovine pancreatic trypsin inhibitor (BPTI) folding intermediate that contains only the disulphide bond between Cys5 and Cys55 has been prepared in Escherichia coli by protein engineering methods, with the other four Cys residues replaced by Ser. disulphide 106-116 spleen trypsin inhibitor I Bos taurus 56-60 1691452-1 1990 The disulphide-bonded intermediates that accumulate in the oxidative folding of bovine pancreatic trypsin inhibitor (BPTI) were characterized some time ago. disulphide 4-14 spleen trypsin inhibitor I Bos taurus 80-115 1691452-1 1990 The disulphide-bonded intermediates that accumulate in the oxidative folding of bovine pancreatic trypsin inhibitor (BPTI) were characterized some time ago. disulphide 4-14 spleen trypsin inhibitor I Bos taurus 117-121 1691452-4 1990 We have tested the hypothesis that the precursor to N* is the one-disulphide intermediate [5-55], which contains the most stable disulphide in BPTI, and present evidence here that this is the case. disulphide 66-76 spleen trypsin inhibitor I Bos taurus 143-147 2466495-1 1988 The possibility that any non-random conformation in reduced bovine pancreatic trypsin inhibitor (BPTI) and ribonuclease A might be significant for folding has been considered, using the experimental data available on forming the first disulphide bond in each. disulphide 235-245 spleen trypsin inhibitor I Bos taurus 97-101 6196487-2 1983 A powerful method of conformational energy minimization which uses both first and second derivatives of the energy function is applied both to a small globular protein, bovine pancreatic trypsin inhibitor (BPTI), consisting of 58 amino acid residues and to its chemical derivative obtained by carboxamidomethylation of cysteinyl residues of the 14-38 disulphide bond. disulphide 351-361 spleen trypsin inhibitor I Bos taurus 206-210