Structure and Dynamics of Cold-Adapted Enzymes as Investigated by FT-IR Spectroscopy and MD. The Case of an Esterase from Pseudoalteromonas haloplanktis

Autor: Aurilia V, Rioux-Dubé JF, Marabotti A, Pézolet M, D'Auria S. Aurilia V, Rioux-Dube' JF, Pezolet M, D'Auria S.

Publikováno v: The journal of physical chemistry. B (1997 : Online) 113 (2009): 7753–7761. doi:10.1021/jp901921r
info:cnr-pdr/source/autori:Aurilia V, Rioux-Dubé JF, Marabotti A, Pézolet M, D'Auria S. Aurilia V, Rioux-Dube' JF, Marabotti A, Pezolet M, D'Auria S./titolo:Structure and dynamics of cold-adapted enzymes as investigated by FT-IR spectroscopy and MD. The case of an esterase from Pseudoalteromonas haloplanktis./doi:10.1021%2Fjp901921r/rivista:The journal of physical chemistry. B (1997 : Online)/anno:2009/pagina_da:7753/pagina_a:7761/intervallo_pagine:7753–7761/volume:113

Enzymes from psychrophiles display high catalytic efficiency at low temperatures. As a consequence, there is a lot of academic and industrial interest in investigating the molecular strategies adopted from these enzymes to work in conditions where ot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1ab85433741675498ccb61342a5d2d4
https://doi.org/10.1021/jp901921r