Title : A transition state "trapped"? QM-cluster models of engineered threonyl-tRNA synthetase.

Pub. Date : 2018 Jun 6

PMID : 29671451






4 Functional Relationships(s)
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1 In a recent study [Science, 2015, 347, 6224], protein engineering was used to design a core within the enzyme threonyl-tRNA synthetase (ThrRS) capable of stabilizing the coplanar transition state conformation of an inserted noncanonical p-biphenylalanine (BiPhe) residue. p-biphenylalanine threonyl-tRNA synthetase 1 Homo sapiens
2 In a recent study [Science, 2015, 347, 6224], protein engineering was used to design a core within the enzyme threonyl-tRNA synthetase (ThrRS) capable of stabilizing the coplanar transition state conformation of an inserted noncanonical p-biphenylalanine (BiPhe) residue. p-biphenylalanine threonyl-tRNA synthetase 1 Homo sapiens
3 In a recent study [Science, 2015, 347, 6224], protein engineering was used to design a core within the enzyme threonyl-tRNA synthetase (ThrRS) capable of stabilizing the coplanar transition state conformation of an inserted noncanonical p-biphenylalanine (BiPhe) residue. p-biphenylalanine threonyl-tRNA synthetase 1 Homo sapiens
4 In a recent study [Science, 2015, 347, 6224], protein engineering was used to design a core within the enzyme threonyl-tRNA synthetase (ThrRS) capable of stabilizing the coplanar transition state conformation of an inserted noncanonical p-biphenylalanine (BiPhe) residue. p-biphenylalanine threonyl-tRNA synthetase 1 Homo sapiens