✦ LIBER ✦

The normal modes of a protein: Native bovine pancreatic trypsin inhibitor

✍ Scribed by Michael Levitt; Christian Sander; Peter S. Stern

Publisher: John Wiley and Sons
Year: 2009
Tongue: English
Weight: 756 KB
Volume: 24
Category: Article
ISSN: 0020-7608
DOI: 10.1002/qua.560240721

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Prediction of protein folding pathways:

Prediction of protein folding pathways: Bovine pancreatic trypsin inhibitor

✍ G. Chelvanayagam; P. Argos 📂 Article 📅 1993 🏛 Springer 🌐 English ⚖ 317 KB

The structure of the complex formed by b

The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor

✍ R. Huber; W. Bode; D. Kukla; U. Kohl; C. A. Ryan 📂 Article 📅 1975 🏛 Springer 🌐 English ⚖ 553 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

Conformation of native, reduced and [5–5

Conformation of native, reduced and [5–55]Ala bovine pancreatic trypsin inhibitor in the gas phase

✍ Victor Nesatiy; Yu-Luan Chen; B. A. Collings; D. J. Douglas 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 109 KB 👁 1 views

Collision cross sections have been measured for gas phase ions of native oxidized bovine pancreatic trypsin inhibitor (BPTI), native reduced BPTI and a mutant form of BPTI containing a single disulphide bond between residues 5 and 55 ([5-55] Ala BPTI). Cross sections for [5-55] Ala BPTI and reduced

Binding of porcine pancreatic secretory

Binding of porcine pancreatic secretory trypsin inhibitor to bovine β-trypsin: A kinetic study

✍ Paolo Ascenzi; Gino Amiconi; Martino Bolognesi; Enea Menegatti; Mario Guarneri 📂 Article 📅 1986 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 530 KB

The kinetics of the formation of the complex between bovine P-trypsin and the porcine pancreatic secretory trypsin inhibitor (PSTI; Kaza-type inhibitor) was investigated following the spectral changes associated with the displacement of proflavine from the enzyme, upon inhibitor binding, between pH

The dynamics of inter-residue distances

The dynamics of inter-residue distances in bovine pancreatic trypsin inhibitor

✍ Wael I. Karain; Basem Ajarmah; Nael I. Qaraeen 📂 Article 📅 2007 🏛 Elsevier Science 🌐 English ⚖ 344 KB