A biologically active 53 kDa fragment of overproduced alanyl-tRNA synthetase from Thermus thermophilus HB8 specifically interacts with tRNA(Ala) acceptor helix

Nucleic Acids Research

Volumn 25, Issue 14, 1997, Pages 2737-2744

  Lechler, Armin ^a   Martin, Andreas ^a   Zuleeg, Tilman ^a   Limmer, Stefan ^a   Kreutzer, Roland ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE TRANSFER RNA; ALANINE TRANSFER RNA LIGASE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; AMINOACYLATION; ARTICLE; CRYSTALLIZATION; ENZYME PURIFICATION; ESCHERICHIA COLI; MICHAELIS CONSTANT; MOLECULAR CLONING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; THERMOSTABILITY; THERMUS THERMOPHILUS;

ALANINE-TRNA LIGASE; AMINO ACID SEQUENCE; CLONING, MOLECULAR; ESCHERICHIA COLI; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; RECOMBINANT FUSION PROTEINS; RNA, TRANSFER, ALA; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; FELIS CATUS; THERMUS THERMOPHILUS;

EID: 0030841037     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/25.14.2737     Document Type: Article

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