✦ LIBER ✦

Relaxation Kinetics and the Glassiness of Proteins: The Case of Bovine Pancreatic Trypsin Inhibitor

✍ Scribed by Baysal, Canan; Atilgan, Ali Rana

Book ID: 118514708
Publisher: Biophysical Society
Year: 2002
Tongue: English
Weight: 135 KB
Volume: 83
Category: Article
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(02)75201-6

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Hydrogen exchange kinetics of bovine pan

Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor .beta.-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, and trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor

✍ Brandt, Pamela; Woodward, Clare 📂 Article 📅 1987 🏛 American Chemical Society 🌐 English ⚖ 826 KB

Relaxation Kinetics and the Glassiness o

Relaxation Kinetics and the Glassiness of Native Proteins: Coupling of Timescales

✍ Baysal, Canan; Atilgan, Ali Rana 📂 Article 📅 2005 🏛 Biophysical Society 🌐 English ⚖ 134 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

Hydrogen Exchange and Protein Hydration:

Hydrogen Exchange and Protein Hydration: The Deuteron Spin Relaxation Dispersions of Bovine Pancreatic Trypsin Inhibitor and Ubiquitin

✍ Vladimir P. Denisov; Bertil Halle 📂 Article 📅 1995 🏛 Elsevier Science 🌐 English ⚖ 831 KB

The normal modes of a protein: Native bo

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

✍ Michael Levitt; Christian Sander; Peter S. Stern 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 756 KB

Influence of thermal motion on 1H chemic

Influence of thermal motion on 1H chemical shifts in proteins: the case of bovine pancreatic trypsin inhibitor

✍ Bernard Busetta; Philippe Picard; Gilles Precigoux 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 115 KB

## Abstract The possible influence of thermal motion on ^1^H chemical shifts is discussed for a small stable protein, the bovine pancreatic Kunitz trypsin inhibitor (BPTI). The thermal effects on the aromatic side chains and on the backbone are treated separately. The thermal motion of the aromatic