Metadata
Title
Biological Soft Matter
Category
general
UUID
c23f4d8ae0b8439eba748681e24e0bbb
Source URL
https://www.tue.nl/en/research/research-groups/self-organizing-soft-matter/impac...
Parent URL
https://www.tue.nl/en/research/research-groups/self-organizing-soft-matter
Crawl Time
2026-03-23T15:15:49+00:00
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Biological Soft Matter

Source: https://www.tue.nl/en/research/research-groups/self-organizing-soft-matter/impacts/biological-soft-matter Parent: https://www.tue.nl/en/research/research-groups/self-organizing-soft-matter

Proteins are amongst the most essential components of all living matter. We study the self-organization of this ‘biological soft matter’ and its effect on their functional and mechanical properties. We are fascinated by ice binding proteins (IBPs) found in certain marine fish, insects, microorganisms and plants. IBPs block ice growth and thus enable life at subzero temperatures. Inspired by these natural cryoprotectants, we develop artificial ice crystal growth modifiers for de-icing and cryopreservation applications. Other examples of our research in this area are single-molecule localization microscopy of (food) proteins at interfaces; thin, large area protein crystals for ultrafast electron diffraction; intrinsically disordered proteins; and enveloped viruses.

Proteins are amongst the most essential components of all living matter. We study the self-organization of this ‘biological soft matter’ and its effect on their functional and mechanical properties. We are fascinated by ice binding proteins (IBPs) found in certain marine fish, insects, microorganisms and plants. IBPs block ice growth and thus enable life at subzero temperatures. Inspired by these natural cryoprotectants, we develop artificial ice crystal growth modifiers for de-icing and cryopreservation applications. Other examples of our research in this area are single-molecule localization microscopy of (food) proteins at interfaces; thin, large area protein crystals for ultrafast electron diffraction; intrinsically disordered proteins; and enveloped viruses.