✦ LIBER ✦

Role of Domains 4 and 5 in Elongation Factor G Functions on the Ribosome

✍ Scribed by Andreas Savelsbergh; Natalia B. Matassova; Marina V. Rodnina; Wolfgang Wintermeyer

Book ID: 115630348
Publisher: Elsevier Science
Year: 2000
Tongue: English
Weight: 228 KB
Volume: 300
Category: Article
ISSN: 0022-2836
DOI: 10.1006/jmbi.2000.3886

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Mutation Analysis of the Role in Ribosom

Mutation Analysis of the Role in Ribosomal Translocation for Loops of Domain IV of the Elongation Factor G

✍ A. V. Kolesnikov; A. T. Gudkov 📂 Article 📅 2003 🏛 SP MAIK Nauka/Interperiodica 🌐 English ⚖ 119 KB

GTPase Activation of Elongation Factors

GTPase Activation of Elongation Factors Tu and G on the Ribosome †

✍ Mohr, Dagmar; Wintermeyer, Wolfgang; Rodnina, Marina V. 📂 Article 📅 2002 🏛 American Chemical Society 🌐 English ⚖ 120 KB

Mutation analysis of the functional role

Mutation analysis of the functional role of amino acid residues in domain IV of elongation factor G

✍ A. A. Kovtun; A. G. Minchenko; A. T. Gudkov 📂 Article 📅 2006 🏛 SP MAIK Nauka/Interperiodica 🌐 English ⚖ 188 KB

Coupling of GTP Hydrolysis by Elongation

Coupling of GTP Hydrolysis by Elongation Factor G to Translocation and Factor Recycling on the Ribosome †

✍ Katunin, Vladimir I.; Savelsbergh, Andreas; Rodnina, Marina V.; Wintermeyer, Wol 📂 Article 📅 2002 🏛 American Chemical Society 🌐 English ⚖ 118 KB

A bacterial elongation factor G homologu

A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi

✍ Takuma Suematsu; Shin-ichi Yokobori; Hiroyuki Morita; Shigeo Yoshinari; Takuya U 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 427 KB

The function of conserved amino acid res

The function of conserved amino acid residues adjacent to the effector domain in elongation factor G

✍ J. Daniel Sharer; Homa Koosha; W. Bret Church; Paul E. March 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 434 KB 👁 1 views

Bacterial elongation factor G (EF-G) physically associates with translocationcompetent ribosomes and facilitates transition to the subsequent codon through the coordinate binding and hydrolysis of GTP. In order to investigate the amino acid positions necessary for EF-G functions, a series of mutatio