Predicting the binding affinities of misacylated tRNAs for Thermus thermophilus EF-Tu.GTP. Journal Article uri icon

Overview

abstract

  • The free energies for the binding of 20 different unmodified Escherichia coli elongator aminoacyl-tRNAs to Thermus thermophilus elongation factor Tu (EF-Tu) were determined. When combined with the binding free energies for the same tRNA bodies misacylated with either valine or phenylalanine determined previously [Asahara, H., and Uhlenbeck, O. C. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 3499-3504], these data permit the calculation of the contribution of each esterified amino acid to the total free energy of binding of the complex. The two data sets can also be used to calculate the free energy of binding of EF-Tu to any misacylated E. coli tRNA, and the values agree well with previously published experimental values. In addition, a survey of active misacylated suppressor tRNAs suggests that a minimal threshold of binding free energy for EF-Tu is required for suppression to occur.

publication date

  • August 1, 2005

has subject area

Date in CU Experts

  • March 13, 2015 12:56 PM

Full Author List

  • Asahara H; Uhlenbeck OC

author count

  • 2

citation count

  • 20

Other Profiles

International Standard Serial Number (ISSN)

  • 0006-2960

Electronic International Standard Serial Number (EISSN)

  • 1520-4995

Additional Document Info

start page

  • 11254

end page

  • 11261

volume

  • 44

issue

  • 33