In this study we investigate the conformational stability of thermophilic esterase 2. MD simulations study allows the identification of two cooperative and coupled domains. Analysis of MD trajectories shows that the last α-helix is the main coupling element.
Molecular dynamics study of the conformational stability of esterase 2 from Alicyclobacillus acidocaldarius / Pagano, Bruno; DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA; Mattia, C. A.; Graziano, G.. - In: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES. - ISSN 0141-8130. - 49:5(2011), pp. 1072-1077. [10.1016/j.ijbiomac.2011.09.002]
Molecular dynamics study of the conformational stability of esterase 2 from Alicyclobacillus acidocaldarius
PAGANO, BRUNO;DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA;
2011
Abstract
In this study we investigate the conformational stability of thermophilic esterase 2. MD simulations study allows the identification of two cooperative and coupled domains. Analysis of MD trajectories shows that the last α-helix is the main coupling element.File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
