A two-step chemical mechanism for ribosome-catalysed peptide bond formation

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

(2011) Hani S Zaher et al.   EMBO JOURNAL

Transition States of Uncatalyzed Hydrolysis and Aminolysis Reactions of a Ribosomal P-Site Substrate Determined by Kinetic Isotope Effects

(2010) David A. Hiller et al.   BIOCHEMISTRY

Validating a new proton shuttle reaction pathway for formation of the peptide bond in ribosomes: A theoretical investigation

(2010) Qiang Wang et al.   CHEMICAL PHYSICS LETTERS

Catalytic Role of Vicinal OH in Ester Aminolysis: Proton Shuttle versus Hydrogen Bond Stabilization

(2010) Miroslav A. Rangelov et al.   JOURNAL OF ORGANIC CHEMISTRY

The transition state for peptide bond formation reveals the ribosome as a water trap

(2010) G. Wallin et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2008) Kevin S. Huang et al.   BIOCHEMISTRY

An Uncharged Amine in the Transition State of the Ribosomal Peptidyl Transfer Reaction

(2008) David A. Kingery et al.   CHEMISTRY & BIOLOGY

Synthesis of Isotopically Labeled P-Site Substrates for the Ribosomal Peptidyl Transferase Reaction

(2007) Minghong Zhong et al.   JOURNAL OF ORGANIC CHEMISTRY