The de novo design of novel artificial proteins that have predictable structures and functions is the most challenging goal in protein design and mimicry. Creating functional artificial metalloproteins requires a detailed understanding of the protein-folding mechanism as well as of the coordination chemistry of the metal centers. Herein we demonstrate a sliding-helix mechanism for stabilizing a change in the ligand environment of DF1, a model di-MnII protein.
Sliding Helix and Change of Coordination Geometry in a Model Di-MnII Protein / Degrado, W. F.; DI COSTANZO, L.; Geremia, S.; Lombardi, Angelina; Pavone, Vincenzo; Randaccio, L.. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 42:4(2003), pp. 417-420. [10.1002/anie.200390127]
Sliding Helix and Change of Coordination Geometry in a Model Di-MnII Protein
L. DI COSTANZO;LOMBARDI, ANGELINA;PAVONE, VINCENZO;
2003
Abstract
The de novo design of novel artificial proteins that have predictable structures and functions is the most challenging goal in protein design and mimicry. Creating functional artificial metalloproteins requires a detailed understanding of the protein-folding mechanism as well as of the coordination chemistry of the metal centers. Herein we demonstrate a sliding-helix mechanism for stabilizing a change in the ligand environment of DF1, a model di-MnII protein.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
