Thread: NMR paper Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
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Default Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.

Related Articles Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.

Peptides. 2002 Dec;23(12):2127-41

Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S

The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the activity of the synthetic peptides IF(1)-(42-58) and IF(1)-(22-46) is correlated to their structure and conformational plasticity determined by CD and [1H]-NMR spectroscopy. Among all the IF(1) segments tested, IF(1)-(42-58) exerts the most potent, pH and temperature dependent activity on the F(o)F(1) complex. The results suggest that, due to its flexible structure, it can fold in helical and/or beta-spiral arrangements that favor the binding to the F(o)F(1) complex, where the native IF(1) binds. IF(1)-(22-46), instead, as it adopts a rigid alpha-helical conformation, it inhibits ATP hydrolysis only in the soluble F(1) moiety.

PMID: 12535691 [PubMed - indexed for MEDLINE]



Source: PubMed
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