Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

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The N-terminal fragment of Acanthamoeba polyphaga mimivirus tyrosyl-tRNA synthetase (TyrRS(apm)) is a monomer in solution.Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS.

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Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

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http://www.wikidata.org/entity/Q39982087

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2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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name

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

@en

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

@nl

type

Item

label

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

@en

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

@nl

prefLabel

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

@en

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

@nl

P1476

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

@en

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Amit Kumar Mandal

http://www.w3.org/2001/XMLSchema#string

Anusree Bhattacharyya

http://www.w3.org/2001/XMLSchema#string

Rajat Banerjee

http://www.w3.org/2001/XMLSchema#string

Rajesh Saha

http://www.w3.org/2001/XMLSchema#string

Siddhartha Roy

http://www.w3.org/2001/XMLSchema#string

Soma Samaddar

http://www.w3.org/2001/XMLSchema#string

Soumi Guha

http://www.w3.org/2001/XMLSchema#string

P2860

Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase

tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase

Architectures of class-defining and specific domains of glutamyl-tRNA synthetase

Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. Possible thermodynamic origins of the "glutamate effect" on protein-DNA interactions.

Quality control mechanisms during translation.

Anticodon and acceptor stem nucleotides in tRNA(Gln) are major recognition elements for E. coli glutaminyl-tRNA synthetase.

Changes in solvation during DNA binding and cleavage are critical to altered specificity of the EcoRI endonuclease

Water release associated with specific binding of gal repressor

The accuracy of aminoacylation--ensuring the fidelity of the genetic code.

Universal rules and idiosyncratic features in tRNA identity.

P304

6035-6042

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scholarly article

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10.1093/NAR/GKG779

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http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

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2003-10-01T00:00:00Z

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274558767

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P698

14530451

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P932

219465

http://www.w3.org/2001/XMLSchema#string

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

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P2860

P2860

Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

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P577

P5875

P698

P932

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P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932