Kell Mortensen – University of Copenhagen

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Center for Synthetic Biology > Meet the Researchers > Kell Mortensen

 

Kell Mortensen

 

 

Title: Professor

Telefon: +45 353-20464

Mobil: +45 2151 6979

E-mail: kell@nbi.ku.dk

Address: Universitetsparken 5, D-03-3-06

2100 København Ø, Denmark

 

 

Read about my research within biophysics and within synthetic biology below

 



Biophysics Research

A main research interest of mine within biophysics is the structural study of macromolecular systems using small-angle x-ray and neutron scattering and static and dynamic light scattering.

In particular, my research group focuses on using these scattering methods to study various types of polymers and colloids. This includes e.g. studying their phase behavior, structural properties and self-assembly. My group also studies the correlation between nano-pores and mechanical behavior as well as dynamics of polymers exposed to elongational stress. We furthermore engage ourselves in: 

✴ Structural properties of star polymers, dendrimers and their self-assembly

✴ Properties of Pluronics, PEO-PPO-PEO, self-assembly and dependence on purity

✴ Polymer fiber structure: correlation between nano-pores and mechanical behavior

✴ Polymer dynamics, melts exposed to elongational stress

✴ Lecithin worm-like microemulsions, structure and micro-rheology

✴ Phospholipid bilayer membranes, and interaction with proteins

✴ Structure / rheology correlation with quality of food products 

✴ Neutron scattering instrumentation, European Spallation Source (ESS)

 

Read more here

Link to publication list

  

Synthetic Biology

 

A promising application of my laboratory's research involves studying synthetic macromolecular systems with the intention of optimizing mechanistic aspects of nano-medicine uptake by cell membranes and the development of platforms for membrane protein studies.

As membrane proteins are the targets for more than half of the pharmaceuticals on the market, we are able to use neutron and X-ray reflection and grazing X-ray diffraction to understand how membrane proteins actually work and to move the borderline for what can be detected.


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