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The well-characterized variant, L99A, of the protein lysozyme from phage T4 was used to identify invisible folded and partially unfolded states by Nuclear Magnetic Resonance (NMR) spectroscopy, among others. (Image: Reproduced and modified with permission from Proc Natl Acad Sci U S A. Copyright 2019 National Academy of Sciences)
Associate Professor Frans Mulder and his research team have published a new study in the renowned journal, Proceedings of the National Academy of Sciences on how proteins can be destabilized by empty spaces in its core. (Photo: private)

2019.10.11 | iNano

Empty spaces, how do they make a protein unstable?

Partial unfolding of proteins can be a big problem in industry, as it may affect the stability of products. So how does an empty space or cavity in its hydrophobic core destabilize a protein? And would such a cavity in fact be empty? These are some of the questions researchers from Aarhus University answer in a new study.

PhD student Alexander B. Jensen receives poster prize at the European Synchrotron Radiation Facility. (Image: Alexander B. Jensen)

2019.10.09 | iNano

PhD student, Alexander B. Jensen, receives poster prize

PhD student in Associate Professor Henrik Birkedals research group receives poster prize at the European Synchrotron Radiation Facility

Malthe von Tangen Sivertsen is the first student to complete the Nanoscience Challenge Programme. (Photo: Jeppe Vang Lauritsen)

2019.10.08 | iNano

First Nanoscience Challenge student

Congratulations to Nanoscience student Malthe von Tangen Sivertsen, who is the first student to have completed the challenge program in nanoscience at Interdisciplinary Nanoscience Center, Aarhus University.

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