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    Destabilizing amyloid fibrils

    Computation analysis identifies six main regions in amyloid proteins that are responsible for their aggregate formation and shows that mutating certain residues can destabilize these amyloid fibers.

    BMC Structural Biology 2015, 15:7
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    Interaction patterns in membrane proteins

    Co-variation in amino acid sequence of intramolecular interaction pairs can be used for structural prediction and classification of unknown transmembrane proteins.

    BMC Structural Biology 2015, 15:6
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    ß-clamp structure from an extremophile

    The crystal structure of the DNA polymerase III beta subunit from Deinococcus radiodurans sheds light on the mechanisms of efficient DNA metabolism that enable this bacterium to survive high doses of radiation.

    BMC Structural Biology 2015, 15:5
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    Leishmania enzyme structure

    The crystal structure of nucleoside diphosphate kinase from the parasite L. braziliensis provides reveals a partially unfolded C-terminus that could serve as a potential target for drug therapies.

    BMC Structural Biology 2015, 15:2
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    Chromatin modification and lysine context

    Molecular modeling of the recognition and modification of histones by the oncogenic NSD class of histone methyl transferases sheds light on the dynamics of these interactions, potentially aiding the design of inhibitors for chemotherapies.

    BMC Structural Biology 2014, 14:25
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