In the last few years, wehave structurally characterized and manipulated TmArgBP that is endowed withseveral unusual features, which include an extraordinary thermal and pressurestability and a remarkable structural versatility [1-7]. In these investigations,the wild-type swapped dimer of TmArgBPwas initially transformed in a monomeric form by deleting its C-terminal helix . This truncated form was further dissectedinto two domains (D1 and D2) that were exhaustively characterized using a repertoireof different experimental and computational techniques . Interestingly, bothD1 and D2 retain the remarkable thermal/chemical stability of the wild-typeprotein . The analysis of the structural and dynamic properties of TmArgBPand of the individual domains have also highlighted possible routes of domaincommunication. Very recently, we also report the development of twoTmArgBP-based different scaffolds for arginine sensing characterized bydifferent sizes and properties .
 Smaldone G,Vigorita M, Ruggiero A,Balasco N, Dattelbaum JD, D'Auria S, Del Vecchio P, Graziano G, Vitagliano L
Biochim Biophys Acta
 Smaldone G, Berisio R, Balasco N, D'AuriaS, Vitagliano L, Ruggiero A.
Biochim Biophys Acta
 Smaldone G, Balasco N, Vigorita M,Ruggiero A, Cozzolino S, Berisio R, Del Vecchio P, Graziano G, Vitagliano L.
IntJ Biol Macromol
 Balasco N, Smaldone G, Vigorita M, DelVecchio P, Graziano G, Ruggiero A, Vitagliano L.
 Smaldone G, Ruggiero A, Balasco N,Abuhammad A, Autiero I, Caruso D, Esposito D, Ferraro G, Gelardi ELM, MoreiraM, Quareshy M, Romano M, Saaret A, Selvam I, Squeglia F, Troisi R,Kroon-Batenburg LMJ, Esposito L, Berisio R, Vitagliano L.
 Jaworek MW, Ruggiero A, Graziano G,Winter R, Vitagliano L.
Phys. Chem. Chem. Phys
 Cozzolino S, Balasco N, Vigorita M,Ruggiero A, Smaldone G, Del Vecchio P, Vitagliano L, Graziano G.
Int J Biol Macromol.
 Smaldone G, Ruggiero A, Balasco N,Vitagliano L.
Int J Mol Sci.
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