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Molecular dynamics simulation and essential dynamics study of mutated plastocyanin: Structural, dynamical and functional effects of a disulfide bridge insertion at the protein surface

TitleMolecular dynamics simulation and essential dynamics study of mutated plastocyanin: Structural, dynamical and functional effects of a disulfide bridge insertion at the protein surface
Publication TypeArticolo su Rivista peer-reviewed
Year of Publication2001
AuthorsArcangeli, Caterina, Bizzarri A.R., and Cannistraro S.
JournalBiophysical Chemistry
Volume92
Pagination183-199
ISSN03014622
KeywordsAlgorithms, article, binding affinity, Chemical analysis, Computer simulation, Copper, Disulfides, electron transport, hydrogen bond, Hydrogen Bonding, Models, Molecular, molecular dynamics, mutant, mutation, plastocyanin, priority journal, Protein, Protein Conformation, Proteins, simulation
Abstract

A molecular dynamics simulation (1.1 ns) at 300 K, of fully hydrated Ile21Cys, Glu25Cys plastocyanin mutant has been performed to investigate the structural, dynamical and functional effects of a disulfide bridge insertion at the surface of the protein. A detailed analysis of the root mean square fluctuations, H-bonding pattern and dynamical cross-correlation map has been performed. An essential dynamics method has also been applied as complementary analysis to identify concerted motions (essential modes), that could be relevant to the electron transfer function. The results have been compared with those previously obtained for wild-type plastocyanin and have revealed that the mutant shows a different pattern of H-bonds, with several interactions lost and a higher flexibility, especially around the electron transfer copper site. The analysis of dynamical cross-correlation map and of essential modes, has shown that the mutant performs different functional concerted motions, which might be related to the binding recognition with its electron transfer partners in comparison with the wild-type protein. © 2001 Elsevier Science B.V. All rights reserved.

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URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0035908899&doi=10.1016%2fS0301-4622%2801%2900199-5&partnerID=40&md5=94b83b74751f43746c8d95ce312c405a
DOI10.1016/S0301-4622(01)00199-5
Citation KeyArcangeli2001183