@article{47e540c06c3711dcbee902004c4f4f50,
title = "Characterization of the residual structure in the unfolded state of the Delta 131 Delta fragment of staphylococcal nuclease",
abstract = "The determination of the conformational preferences in unfolded states of proteins constitutes an important challenge in structural biology. We use inter-residue distances estimated from site-directed spin-labeling NMR experimental measurements as ensemble-averaged restraints in all-atom molecular dynamics simulations to characterise the residual structure of the 131 fragment of staphylococcal nuclease under physiological conditions. Our findings indicate that 131 under these conditions shows a tendency to form transiently hydrophobic clusters similar to those present in the native state of wild-type staphylococcal nuclease. Only rarely, however, all these interactions are simultaneously realized to generate conformations with an overall native topology. Proteins 2006. {\textcopyright} 2006 Wiley-Liss, Inc.",
author = "Francis, {C. J.} and Kresten Lindorff-Larsen and Best, {R. B.} and M. Bendruscolo",
year = "2006",
doi = "10.1002/prot.21077",
language = "English",
volume = "65",
pages = "145--52",
journal = "Proteins: Structure, Function, and Bioinformatics",
issn = "0887-3585",
publisher = "JohnWiley & Sons, Inc.",
number = "1",
}