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1 lubility and strength of interactions of the bovine pancreatic trypsin inhibitor.
2 nted the spontaneous reactivation of reduced bovine pancreatic trypsin inhibitor.
3 in, as well as the less flexible crambin and bovine pancreatic trypsin inhibitor.
4 ids to the N-terminus of chemically modified bovine pancreatic trypsin inhibitor.
5 four internal hydration sites in the protein bovine pancreatic trypsin inhibitor.
6 those in which deviations were observed for bovine pancreatic trypsin inhibitor.
7 ved in molecular dynamics simulations of the bovine pancreatic trypsin inhibitor.
8 izosaccharomyces pombe acid phosphatase, and bovine pancreatic trypsin inhibitor.
9 alization was established using radiolabeled bovine pancreatic trypsin inhibitor (a non-hNE-binding p
10 heterologous multidisulfide proteins, namely bovine pancreatic trypsin inhibitor, a protein with thre
11 lar crowding by two globular proteins, i.e., bovine pancreatic trypsin inhibitor and equine metmyoglo
14 mplex, may be a key factor in the ability of bovine pancreatic trypsin inhibitor and similar inhibito
15 ta) shifts in the two isoleucine residues in bovine pancreatic trypsin inhibitor and the four isoleuc
16 proteins (bovine pancreatic ribonuclease A, bovine pancreatic trypsin inhibitor, and chicken egg whi
17 independently solved structures of barstar, bovine pancreatic trypsin inhibitor, and lysozyme show t
18 ic self-energies of the polar side-chains in bovine pancreatic trypsin inhibitor, and their 666 inter
19 are inhibited by soybean trypsin inhibitor, bovine pancreatic trypsin inhibitor, antithrombin III, a
20 are in contrast to large values reported for bovine pancreatic trypsin inhibitor at more extreme cond
21 f a complex formed between a cleaved form of bovine pancreatic trypsin inhibitor (BPTI) and a catalyt
22 milar to the published crystal structures of bovine pancreatic trypsin inhibitor (BPTI) and alpha-DtX
23 ke mutations for resistance to inhibition by bovine pancreatic trypsin inhibitor (BPTI) and amyloid p
24 two opposite extreme models, represented by bovine pancreatic trypsin inhibitor (BPTI) and hirudin.
26 ino acid residues in the reactive surface of bovine pancreatic trypsin inhibitor (BPTI) and surroundi
27 Partially folded conformational ensembles of bovine pancreatic trypsin inhibitor (BPTI) are accessed
29 the behavior of equine metmyoglobin (Mb) and bovine pancreatic trypsin inhibitor (BPTI) at concentrat
30 ns molecular dynamics simulations of reduced bovine pancreatic trypsin inhibitor (BPTI) at high tempe
31 -ray crystal structure of the thrombin E192Q-bovine pancreatic trypsin inhibitor (BPTI) complex, the
32 A point mutation, G37A, on the surface of bovine pancreatic trypsin inhibitor (BPTI) destabilizes
39 wed us to chemically link a terminal 6.5-kDa bovine pancreatic trypsin inhibitor (BPTI) moiety to prO
40 versibly inhibited with a potent (Ki=0.4 nM) bovine pancreatic trypsin inhibitor (BPTI) mutant (5L15)
41 ous Kunitz-type inhibitors homologous to the bovine pancreatic trypsin inhibitor (BPTI) provide a sui
42 Co-expression of rPDI increased the yield of bovine pancreatic trypsin inhibitor (BPTI) severalfold,
45 cid replacements on the backbone dynamics of bovine pancreatic trypsin inhibitor (BPTI) were examined
46 ly synthesized partially folded analogues of bovine pancreatic trypsin inhibitor (BPTI) with the prot
49 )) contain an intracellular binding site for bovine pancreatic trypsin inhibitor (BPTI), a well-known
51 he native-like two-disulfide intermediate of bovine pancreatic trypsin inhibitor (BPTI), with the dis
58 rnally applied serine proteinase inhibitors: bovine pancreatic trypsin inhibitor (BPTI, KD = 7.0 micr
59 ier alanine-scanning experiment conducted on bovine pancreatic trypsin inhibitor (BPTI; 58 residues)
60 ple simulations of three different proteins, bovine pancreatic trypsin inhibitor, chymotrypsin inhibi
61 alculations are performed for five proteins: bovine pancreatic trypsin inhibitor, cytochrome c, plast
62 ctivity with DTT; however, partially reduced bovine pancreatic trypsin inhibitor (des(14-38)) is not.
63 small (approximately 6- to 7-kDa) peptides, bovine pancreatic trypsin inhibitor, epidermal growth fa
66 g reversible association of chymotrypsin and bovine pancreatic trypsin inhibitor in a solution mixtur
67 tions of coexisting monomers and decamers of bovine pancreatic trypsin inhibitor in the presence of d
71 ade between the structures of P1 (Lys+)15 of bovine pancreatic trypsin inhibitor (Kunitz) ( and ) and
72 Eglin c, turkey ovomucoid third domain, and bovine pancreatic trypsin inhibitor (Kunitz) are all sta
74 racterized, indicating the presence of three bovine pancreatic trypsin inhibitor/Kunitz domains and i
75 he disulfide bond between Cys14 and Cys38 of bovine pancreatic trypsin inhibitor lies on the surface
77 orded for samples containing up to 0.12 g/mL bovine pancreatic trypsin inhibitor or 0.2 g/mL metmyogl
78 plexed with either of the smaller inhibitors bovine pancreatic trypsin inhibitor or turkey ovomucoid
79 ically a 28 amino acid fragment derived from bovine pancreatic trypsin inhibitor, or misfolded protei
81 substrate dynamics in the cleavage of Kunitz-bovine pancreatic trypsin inhibitor protease inhibitors
82 0 microM polylysine) ECaSt/PDI augmented the bovine pancreatic trypsin inhibitor reactivation rate.
83 ing of KD1 based on the crystal structure of bovine pancreatic trypsin inhibitor revealed that KD1 fo
84 lar dynamics simulation of the small protein bovine pancreatic trypsin inhibitor reveals that its mai
85 ins (chymotrypsinogen, pepsinogen, lysozyme, bovine pancreatic trypsin inhibitor, ribonuclease A, and
86 tein, shows that the dramatic enhancement of bovine pancreatic trypsin inhibitor self-association can
88 ns: hen egg-white lysozyme, equine lysozyme, bovine pancreatic trypsin inhibitor, staphylococcal nucl
89 1 residue of the bound inhibitors ecotin and bovine pancreatic trypsin inhibitor suggested that the m
90 ned a library encoding random mutations in a bovine pancreatic trypsin inhibitor variant containing a
92 ies for plasmin of the plasmin inhibitor and bovine pancreatic trypsin inhibitor were reduced by conj
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