Minimal Transition State Charge Stabilization of the Oxyanion during Peptide Bond Formation by the Ribosome-Reference-Cited by-同舟云学术

Minimal Transition State Charge Stabilization of the Oxyanion during Peptide Bond Formation by the Ribosome

Published:2011-11-09 Issue:48 Volume:50 Page:10491-10498
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Carrasco Nicolas¹,Hiller David A.¹,Strobel Scott A.¹

Affiliation:

1. Departments of Molecular Biophysics & Biochemistry and Chemistry, Yale University, 260 Whitney Ave., New Haven, Connecticut 06520-81114, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi201290s

Reference49 articles.

1. What recent ribosome structures have revealed about the mechanism of translation

2. The Structural Basis of Ribosome Activity in Peptide Bond Synthesis

3. Substrate-assisted catalysis of peptide bond formation by the ribosome

4. The 2′-OH group of the peptidyl-tRNA stabilizes an active conformation of the ribosomal PTC

5. Transition State Chirality and Role of the Vicinal Hydroxyl in the Ribosomal Peptidyl Transferase Reaction

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4. Mechanistic Insights Into Catalytic RNA–Protein Complexes Involved in Translation of the Genetic Code;Structural and Mechanistic Enzymology;2017

5. Induced fit of the peptidyl-transferase center of the ribosome and conformational freedom of the esterified amino acids;RNA;2016-11-22