Molecular dynamics simulations of Hydrogenobacter thermophilus cytochrome c552: comparisons of the wild-type protein, a b-type variant, and the apo state.

Journal article

Molecular dynamic simulations have been performed for wild-type Hydrogenobacter thermophilus cytochrome c(552), a b-type variant of the protein, and the apo state with the heme prosthetic group removed. In the b-type variant, Cys 10 and Cys 13 were mutated to alanine residues, and so the heme group was no longer covalently bound to the protein. Two 8-ns simulations have been performed for each system at 298 and 360 K. The simulations of the wild-type protein at 298 K show a very close agreeme...

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Authors: Smith, L; Davies, R; van Gunsteren, W

• Publication status: Published
• Journal: Proteins
• Volume: 65
• Issue: 3
• Pages: 702-711
• Publication date: 2006-11-01
• DOI: 10.1002/prot.21141
• EISSN: 1097-0134
• ISSN: 0887-3585
• Language: English
• Keywords: Binding Sites; Models, Molecular; Protein Structure, Secondary; Magnetic Resonance Spectroscopy; Alanine; Cysteine; Apoproteins; Cytochrome c Group; Bacterial Proteins; Hydrogen Bonding