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Lund University
 

Akke Research Group

Group members

  • Mikael Akke, professor
  • Anna Bille, associated PhD student (Department of Theoretical Physics)
  • Kristine Steen Jensen, postdoc
  • Kristofer Modig, lecturer
  • Olof Stenström, PhD student
  • Johan Wallerstein, PhD student
  • Ulrich Weininger, postdoc

Current projects

Conformational entropy in ligand binding and drug design

NMR relaxation methods for aromatic side chains

Conformational dynamics and enzyme catalysis

Partial unfolding and transient oligomerization of superoxide dismutase

Recent publications

Ring flips revisited: 13C relaxation dispersion measurements of aromatic side chain dynamics and activation barriers in Basic Pancreatic Trypsin Inhibitor. Weininger U, Modig K, Akke M. Biochemistry 53, 4519–4525 (2014). 

Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection. Weininger U, Brath U, Modig K, Teilum K, Akke M. J. Biomol. NMR 59, 23–29 (2014). 

Slow aromatic ring flip detected despite near-degenerate NMR frequencies of the exchanging nuclei. Weininger U, Respondek M, Löw C, Akke M. J. Phys. Chem. B 117, 9241–9247 (2013). 

Local unfolding and aggregation mechanism of SOD1 — a Monte-Carlo exploration. Bille A, Jonsson SÆ, Akke M, Irbäck A. J. Phys. Chem. B 117, 9194–9202 (2013). 

Protein conformational exchange measured by 1H R relaxation dispersion of methyl groups. Weininger U, Blissing AT, Hennig J, Ahlner A, Liu Z, Vogel HJ, Akke M, Lundström P. J. Biomol. NMR 57, 47–55 (2013). 

The carbohydrate binding site in Galectin-3 is preorganized to recognize a sugar-like framework of oxygens: ultra-high resolution structures and water dynamics. Saraboji K, Genheden S, Diehl C, Qvist J, Weininger U, Nilsson UJ, Leffler H, Ryde U, Akke M, Logan D. Biochemistry 51, 296–306 (2012). 

Specific 12CβD212CγD2S13CγHD2 isotopomer labeling of methionine to characterize protein dynamics by 1H and 13C NMR relaxation dispersion. Weininger U, Liu Z, McIntyre DD, Vogel HJ, Akke M. J. Am. Chem. Soc. 134, 18562–18565 (2012). 

Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected 13C CPMG relaxation dispersion. Weininger U, Respondek M, Akke M. J. Biomol. NMR 54, 9–14 (2012). 

13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy. Weininger U, Diehl C, Akke M. J. Biomol. NMR 53, 181–190 (2012). 

Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3. Diehl C, Engström O, Delaine T, Håkansson M, Genheden S, Modig K, Leffler H, Ryde U, Nilsson UJ, Akke M. J. Am. Chem. Soc. 132, 14577–14589 (2010). 

Structure and dynamics of ribosomal protein L12: an ensemble model based on SAXS and NMR relaxation. Bernado P, Modig K, Grela P, Svergun D, Tchorzewski M, Pons M, Akke M. Biophys. J. 98, 2374–2382 (2010). 

 

 

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Last updated: 2014-10-06