• Universal clamping protein stabilizes folded proteins

    New insight into how the chaperone protein Hsp70 works On October 26th Nature will publish a study that overturns the decades-old textbook model of action for a protein that is …

    Read more

  • Universeel klemeiwit stabiliseert andere eiwitten

    Nieuw inzicht in werkingsmechanisme chaperonne-eiwit Hsp70 Op 26 oktober publiceert Nature een onderzoek dat een decennia oud model voor de werking van een cruciaal eiwit omverwerpt. Onderzoekers van FOM-instituut AMOLF …

    Read more

  • Change accelerates stalled evolution

    Researchers of FOM Institute AMOLF and Laboratoire Interdisciplinaire de Physique in Grenoble (France) have shown that the evolution of bacteria can be accelerated when their environment fluctuates in time. The research …

    Read more

  • Verandering versnelt vastgelopen evolutie

    Onderzoekers van FOM-instituut AMOLF en Laboratoire Interdisciplinaire de Physique in Grenoble (Frankrijk) hebben ontdekt dat de evolutie van een bacterie versnelt als de leefomgeving veranderlijk is. Het onderzoek geeft een …

    Read more

  • New 3D tracking technique “for the masses” reveals individuality of bacterial behavior

    Microscopy techniques used to study the movement of swimming microbes are limited to two dimensions (2D) or require sophisticated devices. In a paper to be published online on 2 November, …

    Read more

  • Katja Taute wins award for outstanding talk

    AMOLF postdoc Katja Taute (Systems Biology and Biophysics research groups) has won the award for outstanding postdoctoral talk at the BLAST XIII conference  (13th International Conference on Bacterial Locomotion and …

    Read more

  • Cell factory runs with fits and starts

    Researchers from FOM institute AMOLF have discovered that metabolism, the process that converts molecules in a cell, proceeds irregularly. As metabolism is the motor that drives all biological activity in …

    Read more

  • Observing the misfolding of a single protein

    Researchers from FOM institute AMOLF have directly observed the misfolding of a protein chain. Protein chains are thought to fold into the wrong structure sometimes, and thus cause neurodegenerative diseases.

    Read more