๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Structure of an intermediate in the unfolding of creatine kinase

โœ Scribed by Timothy I. Webb; Glenn E. Morris

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
404 KB
Volume
42
Category
Article
ISSN
0887-3585

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

Role of quaternary structure in muscle c
Role of quaternary structure in muscle creatine kinase stability: Tryptophan 210 is important for dimer cohesion
โœ Catherine Perraut; Eric Clottes; Chantal Leydier; Christian Vial; Olivier Marcil ๐Ÿ“‚ Article ๐Ÿ“… 1998 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 111 KB ๐Ÿ‘ 1 views

A mutant of the dimeric rabbit muscle creatine kinase (MM-CK) in which tryptophan 210 was replaced has been studied to assess the role of this residue in dimer cohesion and the importance of the dimeric state for the native enzyme stability. Wild-type protein equilibrium unfolding induced by guanidi

The Structure of the Intermediate in Ele
The Structure of the Intermediate in Electrophilic Aromatic Substitutions
โœ H. Zollinger ๐Ÿ“‚ Article ๐Ÿ“… 1963 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 265 KB ๐Ÿ‘ 2 views

Presence of oxidizing agents, these reactions are retarded and the P-P bonds in the sulfides, whose presence was demonstrated Some years ago by X-ray structural analysis, remain unaltered. Since the P-P bonds in phosphorus oxyacids are stable in alkaline solution and in order to avoid the presence o