The function of conserved amino acid residues adjacent to the effector domain in elongation factor G

Proteins: Structure, Function and Genetics

Volumn 37, Issue 2, 1999, Pages 293-302

  Sharer, J Daniel ^a   Koosha, Homa ^a   Church, W Bret ^a   March, Paul E ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

E. coli; Electrostatic potential; fusA; Homology modeling; Mutagenesis; Ribosomes; Surface charge; Translation

Indexed keywords

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; CROSS LINKING; ESCHERICHIA COLI; GENE TRANSLOCATION; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CROSS-LINKING REAGENTS; ELECTROSTATICS; ESCHERICHIA COLI; GUANOSINE TRIPHOSPHATE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE ELONGATION FACTOR G; POLYMERASE CHAIN REACTION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RIBOSOMES; ULTRAVIOLET RAYS;

EID: 0032740154     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991101)37:2<293::AID-PROT14>3.0.CO;2-3     Document Type: Article

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