✦ LIBER ✦

Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE

✍ Scribed by Yves Bourne; Zoran Radić; Hartmuth C. Kolb; K. Barry Sharpless; Palmer Taylor; Pascale Marchot

Book ID: 113517222
Publisher: Elsevier Science
Year: 2005
Tongue: English
Weight: 260 KB
Volume: 157-158
Category: Article
ISSN: 0009-2797
DOI: 10.1016/j.cbi.2005.10.018

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

The Structure of Truncated Recombinant H

The Structure of Truncated Recombinant Human Bile Salt-stimulated Lipase Reveals Bile Salt-independent Conformational Flexibility at the Active-site Loop and Provides Insights into Heparin Binding

✍ Stanley A. Moore; Richard L. Kingston; Kerry M. Loomes; Olle Hernell; Lars Bläck 📂 Article 📅 2001 🏛 Elsevier Science 🌐 English ⚖ 648 KB

Structure of the complex between trypano

Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: Binding at the active site despite an “open” flexible loop conformation

✍ Christophe L.M.J. Verlinde; Cornelis J. Witmans; Tjaard Pijning; Kor H. Kalk; Wi 📂 Article 📅 1992 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 711 KB

## Abstract The structure of triosephosphate isomerase from __Trypanosoma brucei__ complexed with the competitive inhibitor __N__‐hydroxy‐4‐phosphono‐butanamide was determined by X‐ray crystallography to a resolution of 2.84 å. Full occupancy binding of the inhibitor is observed only at one of the