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DEPLETION AND REPLACEMENT OF PROTEIN METAL LIGANDS
Author(s): BARRICK D
Source: CURRENT OPINION IN BIOTECHNOLOGY    Volume: 6    Issue: 4    Pages: 411-418    Published: AUG 1995  
Times Cited: 24     References: 59     
Abstract: Recently, site-directed mutagenesis has been applied to protein-derived metal ligands in a way that permits the replacement in trans of protein ligands. The chemical diversity of ligands available using this method far exceeds that attainable using standard mutagenesis. Non-conservative ligand replacement can yield novel metalloproteins with altered ligand-binding, enzymatic activities, and spectroscopic properties. Conservative ligand substitution, or 'ligand detachment', allows the structural and functional effects of the covalent linkage between the ligand and the protein to be evaluated; this linkage is often proposed to play a critical role in modulating the structure and reactivity of the metal center. Furthermore, this method can be exploited to study the details of molecular recognition at the structural, thermodynamic, and dynamic levels.
Document Type: Article
Language: English
Reprint Address: BARRICK, D (reprint author), UNIV OREGON, INST MOLEC BIOL, EUGENE, OR 97403 USA
Publisher: CURRENT BIOLOGY LTD, 34-42 CLEVELAND STREET, LONDON, ENGLAND W1P 6LB
Subject Category: Biochemical Research Methods; Biotechnology & Applied Microbiology
IDS Number: RM837
ISSN: 0958-1669
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