Mg2+-Free Bacillus stearothermophilus Tryptophanyl-tRNA Synthetase Retains a Major Fraction of the Overall Rate Enhancement for Tryptophan Activation
Author:
Affiliation:
1. Department of Biochemistry and Biophysics, CB 7260, University of North Carolina, Chapel Hill, North Carolina 27599-7260
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja076557x
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1. Domain acquisition by class I aminoacyl-tRNA synthetase urzymes coordinated the catalytic functions of HVGH and KMSKS motifs;Nucleic Acids Research;2023-07-20
2. High-throughput thermal denaturation of tryptophanyl-tRNA synthetase combinatorial mutants reveals high-order energetic coupling determinants of conformational stability;Structural Dynamics;2023-07-01
3. Microcalorimetry reveals multi-state thermal denaturation of G. stearothermophilus tryptophanyl-tRNA synthetase;Structural Dynamics;2023-07-01
4. Domain Acquisition by Class I Aminoacyl-tRNA Synthetase Urzymes Coordinated the Catalytic Functions of HVGH and KMSKS Motifs;2023-04-26
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