Copper (II) tuning interactions of amylin fragments with artificial membranes: a DSC study

Autor: Grasso, D, Miliardi, D, LA ROSA, Carmelo, Impellizzeri, G, Pappalardo, G, Magrì, A, Rizzarelli, Enrico

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______4731::38b7f917f11975d0a2d03eea1b78326e
http://hdl.handle.net/20.500.11769/246233

Structural Zn(II) implies a switch from fully cooperative to partly downhill folding in highly homologous proteins

Autor: Danilo Milardi, Maddalena Palmieri, Sabrina Esposito, Annarita Del Gatto, Fortuna Netti, Roberto Fattorusso, Paolo V. Pedone, Luigi Russo, Laura Zaccaro, Carla Isernia, Gaetano Malgieri, Ilaria Baglivo, Ivan de Paola

Publikováno v: Journal of the American Chemical Society
135 (2013): 5220–5228. doi:10.1021/ja4009562
info:cnr-pdr/source/autori:Palmieri, M ; Malgieri, G ; Russo, L ; Baglivo, I ; Esposito, S ; Netti, F ; Del Gatto, A ; de Paola, I ; Zaccaro, L ; Pedone, PV ; Isernia, C ; Milardi, D ; Fattorusso, R ./titolo:Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins/doi:10.1021%2Fja4009562/rivista:Journal of the American Chemical Society (Print)/anno:2013/pagina_da:5220/pagina_a:5228/intervallo_pagine:5220–5228/volume:135

In the funneled landscape, proteins fold to their native states through a stochastic process in which the free energy decreases spontaneously and unfolded, transition, native, and possible intermediate states correspond to local minima or saddle poin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::974b04f5f6cea87666de2c065c04ecf6
https://pubmed.ncbi.nlm.nih.gov/23484956