✦ LIBER ✦

The 5–55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor

✍ Scribed by N.J. Darby; C.P.M. van Mierlo; T.E. Creighton

Book ID: 115924574
Publisher: Elsevier Science
Year: 1991
Tongue: English
Weight: 506 KB
Volume: 279
Category: Article
ISSN: 0014-5793
DOI: 10.1016/0014-5793(91)80251-w

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

A third native one-disulphide intermedia

A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor

✍ Dadlez, Michal; Kim, Peter S. 📂 Article 📅 1995 🏛 Nature Publishing Group 🌐 English ⚖ 467 KB

A new two-disulphide intermediate in the

A new two-disulphide intermediate in the refolding of reduced bovine pancreatic trypsin inhibitor

✍ D.J. States; C.M. Dobson; M. Karplus; T.E. Creighton 📂 Article 📅 1984 🏛 Elsevier Science 🌐 English ⚖ 611 KB

The stabilizing effects of hydrophobic c

The stabilizing effects of hydrophobic cores on peptide folding of bovine-pancreatic-trypsin-inhibitor folding-intermediate model

✍ Dae Young KWON; Peter S. KIM 📂 Article 📅 1994 🏛 John Wiley and Sons 🌐 English ⚖ 541 KB

Folding of the twisted .beta.-sheet in b

Folding of the twisted .beta.-sheet in bovine pancreatic trypsin inhibitor

✍ Chou, Kuo Chen; Nemethy, George; Pottle, Marcia S.; Scheraga, Harold A. 📂 Article 📅 1985 🏛 American Chemical Society 🌐 English ⚖ 691 KB

1H NMR Analysis of the Partly-folded Non

1H NMR Analysis of the Partly-folded Non-native Two-disulphide Intermediates (30-51,5-14) and (30-51,5-38) in the Folding Pathway of Bovine Pancreatic Trypsin Inhibitor

✍ Carlo P.M. van Mierlo; Johan Kemmink; David Neuhaus; Nigel J. Darby; Thomas E. C 📂 Article 📅 1994 🏛 Elsevier Science 🌐 English ⚖ 807 KB

Multiple intermediates in the reaction o

Multiple intermediates in the reaction of bovine β-trypsin with bovine pancreatic trypsin inhibitor (kunitz)

✍ Eraldo Antonini; Paolo Ascenzi; Enea Menegatti; Mario Guarneri 📂 Article 📅 1983 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 630 KB

The kinetics of the formation of the complex between bovine P-trypsin and the bovine basic pancreatic trypsin inhibitor (BPTI) was investigated using three different signals: the displacement of proflavine, the optical density changes in the UV region, and the loss of the enzymatic activity. For the