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- Title
Dynamics and unfolding pathway of chimeric azurin variants: insights from molecular dynamics simulation.
- Authors
Evoli, Stefania; Guzzi, Rita; Rizzuti, Bruno
- Abstract
The spectroscopic, thermal, and functional properties of blue copper proteins can be modulated by mutations in the metal binding loop. Molecular dynamics simulation was used to compare the conformational properties of azurin and two chimeric variants, which were obtained by inserting into the azurin scaffold the copper binding loop of amicyanin and plastocyanin, respectively. Simulations at room temperature show that the proteins retain their overall structure and exhibit concerted motions among specific inner regions, as revealed by principal component analysis. Molecular dynamics at high temperature indicates that the first events in the unfolding pathway are structurally similar in the three proteins and unfolding starts from the region of the α-helix that is far from the metal binding loop. The results provide details of the denaturation process that are consistent with experimental data and in close agreement with other computational approaches, suggesting a distinct mechanism of unfolding of azurin and its chimeric variants. Moreover, differences observed in the dynamics of specific regions in the three proteins correlate with their thermal behavior, contributing to the determination of the basic factors that influence the stability. Graphical abstract: [Figure not available: see fulltext.]
- Subjects
AZURINS; MOLECULAR dynamics; COPPER proteins; PROTEIN folding; SPECTRUM analysis; GENETIC mutation; CONFORMATIONAL analysis
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2013, Vol 18, Issue 7, p739
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-013-1017-1