Effect of the Central Disulfide Bond on the Unfolding Behavior of Elongation Factor Ts Homodimer from Thermus thermophilus-Reference-Cited by-同舟云学术

Effect of the Central Disulfide Bond on the Unfolding Behavior of Elongation Factor Ts Homodimer from Thermus thermophilus

Published:2001-07-20 Issue:32 Volume:40 Page:9579-9586
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sedlák Erik¹,Valušová Eva¹,Nesper-Brock Martina¹,Antalík Marián¹,Sprinzl Mathias¹

Affiliation:

1. Department of Biochemistry, Faculty of Science P. J. Šafárik University, Košice, Slovakia, Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Košice, Slovakia, and Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi010274e

Reference53 articles.

1. Dimers of Thermus thermophilus elongation factor Ts are required for its function as a nucleotide exchange factor of elongation factor Tu

2. Elongation Factor Ts from Thermus thermophilus. Overproduction in Escherichia coli, Quaternary Structure and Interaction with Elongation Factor Tu

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