Calculation of the redox potential of the protein azurin and some mutants

Autor: M. van den Bosch, W.F.van Gunsteren, Marcel Swart, Hjc Berendsen, Gerard W. Canters, Alan E. Mark, Chris Oostenbrink, J. G. Snijders

Publikováno v: ChemBioChem, 6(4), 738-46. Wiley-VCH Verlag
van den Bosch, M, Swart, M, Snijders, J G, Berendsen, H J, Mark, A E, Oostenbrink, C, van Gunsteren, W F & Canters, G W 2005, ' Calculation of the redox potential of the protein azurin and some mutants ', ChemBioChem, vol. 6, no. 4, pp. 738-46 . https://doi.org/10.1002/cbic.200400244
ChemBioChem, 6(4), 738-746. WILEY-V C H VERLAG GMBH

Azurin from Pseudomonas aeruginosa is a small 128-residue, copper-containing protein. Its redox potential can be modified by mutating the protein. Free-energy calculations based on classical molecular-dynamics simulations of the protein and from muta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b548d45b548e4721e162b6cc258591c7
https://doi.org/10.1002/cbic.200400244

Comparison of estimates of free energy for binding of mono- and di-substituted benzenes with α-cyclodextrin obtained by single-step perturbation and thermodynamic integration

Autor: Musa I. El-Barghouthi, Mohammad B. Zughul, Adnan A. Badwan, W.F.van Gunsteren, Merijn Schenk

Publikováno v: Journal of Inclusion Phenomena and Macrocyclic Chemistry. 57:375-377

In this work, the relative free energies of binding individual members of a series of mono- and di-substituted benzenes to α-cyclodextrin in water have been estimated using the single step perturbation methodology (SSP). The computations involved we

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2f5cf55ac983d1fd2552d243f26621a5
https://doi.org/10.1007/s10847-006-9257-0

Decomposition of the Free Energy of a System in Terms of Specific Interactions

Autor: W.F.van Gunsteren, Alan E. Mark

Publikováno v: Journal of Molecular Biology. 240:167-176

Recently, a number of methods have been proposed that are designed to extract contributions to the change in free energy associated with a given perturbation or mutation of a protein originating from specific residue-residue or atom-atom interactions

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::80acaf717e61ee28bc824db2c92af616
https://doi.org/10.1006/jmbi.1994.1430

Temperature and urea induced denaturation of the TRP-cage mini protein TC5b: A simulation study consistent with experimental observations

Autor: Zrinka Gattin, Sereina Riniker, P. J. Hore, W.F.van Gunsteren, K. H. Mok

Publikováno v: Protein science : a publication of the Protein Society. 18(10)

The effects of temperature and urea denaturation (6M urea) on the dominant structures of the 20-residue Trp-cage mini-protein TC5b are investigated by molecular dynamics simulations of the protein at different temperatures in aqueous and in 6M urea s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9515de951a4b81143559413ee22365d5
http://ora.ox.ac.uk/objects/uuid:1e77c355-dc00-44e6-8a00-09f97a65b6c9

Molecular dynamics simulations of peptide fragments from hen lysozyme: insight into non-native protein conformations

Autor: Christopher M. Dobson, Lorna J. Smith, Alan E. Mark, W.F.van Gunsteren

Publikováno v: Journal of molecular biology. 280(4)

Molecular dynamics simulations of four peptides taken from the hen lysozyme sequence have been used to generate models for non-native protein conformations. Comparisons between the different peptides and with experimental data for denatured lysozyme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d63b65d0ce9f099e9296cc07681720b
http://ora.ox.ac.uk/objects/uuid:a76106c7-1b2f-41dc-a45a-a72495352077