Read Online Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10. - Poger, David; Fuchs, Jean-François; Nedev, Hristo; Ferrand, Michel; Crouzy, Serge file in ePub Online

Download Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10. - Poger, David; Fuchs, Jean-François; Nedev, Hristo; Ferrand, Michel; Crouzy, Serge | ePub

Genre/Form: article in peer-reviewed journal Material Type: Internet resource Document Type: Internet Resource, Archival Material All Authors / Contributors: Poger, David; Fuchs, Jean-François; Nedev, Hristo; Ferrand, Michel; Crouzy, Serge OCLC Number: 798350487 Language Note: English Abstract: Molecular dynamics simulations were performed on both apo and copper forms of the human copper chaperone, Hah1. Wild-type Hah1 and a methionine (M10) to serine mutant were investigated. We have evidenced the central role of residue M10 in stabilizing the hydrophobic core of Hah1 as well as the internal structure of the metal-binding site. When copper(I) is bound, the mobility of Hah1 is reduced whereas mutation of M10 implies a drastic increase of the mobility of apoHah1, stressing the importance of this highly conserved hydrophobic residue for copper sequestration by the apoprotein.

Title : Molecular dynamics study of the metallochaperone Hah1 in its apo and Cu(I)-loaded states: role of the conserved residue M10.
Author : Poger, David; Fuchs, Jean-François; Nedev, Hristo; Ferrand, Michel; Crouzy, Serge
Language : en
Rating :
4.90 out of 5 stars
Type : PDF, ePub, Kindle
Uploaded : Apr 12, 2021

Post Your Comments: