Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 325, Issue 4, Pages 1271-1278Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2004.10.144
Keywords
apo-metallothionein; molecular dynamics; protein folding; de novo synthesis; post-translational metallation
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We report the first molecular dynamics calculations on the structure of metal-free Pot recombinant human metallothionein, with comparison to the two isolated fragments, alpha-rhMT and beta-rhNIT, starting from a linear synthesized strand as well as a demetallated conformation. Following a 5000 ps MM3/MD calculation, the cysteine side chains were found to populate the outside surface of the metal-free protein, regardless of the initial conformation. The polypeptide backbone adopted a random coil conformation when starting from the linear strand, however, it retained a significant amount of secondary structure when starting from the demetallated conformation. We propose that the inverted cysteinyl sulfur orientation facilitates the binding of the metal ions to form the proteolytically stable, metallated protein. (C) 2004 Elsevier Inc. All rights reserved.
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