Enhanced complexity and catalytic efficiency in the hydrolysis of phosphate diesters by rationally designed helix-loop-helix motifs

ChemBioChem

Volumn 9, Issue 12, 2008, Pages 1975-1984

  Razkin, Jesus ^c   Lindgren, Johan ^a   Nilsson, Helena ^b   Baltzer, Lars ^a  

^a UPPSALA UNIVERSITY   (Sweden)

^b LINKÖPING UNIVERSITY   (Sweden)

^c PUBLIC UNIVERSITY OF NAVARRE   (Spain)

Author keywords

Catalysis; De nova design; Hydrolysis; Peptides; Phosphodiesters

Indexed keywords

4 NITROPHENYL PHOSPHATE; ALKYL ARYL PHOSPHATE; DNA; HISTIDINE; IMIDAZOLE; ORGANOPHOSPHATE; PEPTIDE HJ1; PHOSPHATE; POLYPEPTIDE; RNA; TYROSINE; UNCLASSIFIED DRUG; URIDINE 3' 2,2,2 TRICHLOROETHYL PHOSPHATE;

ACID BASE BALANCE; AMINO ACID ANALYSIS; AQUEOUS SOLUTION; ARTICLE; CATALYSIS; CHEMICAL REACTION; CONTROLLED STUDY; DNA BINDING MOTIF; DNA CLEAVAGE; DNA HELIX; ENZYME ACTIVE SITE; ENZYME MECHANISM; HYDROLYSIS; MOLECULAR STABILITY; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; RESIDUE ANALYSIS; RNA CLEAVAGE;

AMINO ACID SEQUENCE; BINDING SITES; BIOMIMETIC MATERIALS; CATALYSIS; DIMERIZATION; DNA; DRUG DESIGN; ESTERS; HELIX-LOOP-HELIX MOTIFS; HYDROLYSIS; HYDROPHOBICITY; PEPTIDES; PHOSPHATES; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; SALTS;

EID: 54349095412     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200800057     Document Type: Article

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