Home  |  
Style  |  
Sitemap  |  
Svenska  |  
Lund University

Akke Research Group

Group members

  • Mikael Akke, professor
  • Anna Bille, associated PhD student (Department of Theoretical Physics)
  • Mikael Carlsson, diploma student
  • Ashhar Khan, visiting PhD student from IIT-Delhi
  • 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

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). 

Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization. Teilum K, Smith MH, Schultz E, Christensen LC, Solomentsev G, Oliveberg M, Akke M. Proc. Natl. Acad. Sci. U.S.A. 106, 18273–18278 (2009).

Conformational entropy changes upon lactose binding to the carbohydrate recognition domain of galectin-3. Diehl C, Genheden S, Modig K, Ryde U, Akke M.  J. Biomol. NMR 45, 157–169 (2009).

Differential response of the backbone and side chain conformational dynamics in FKBP12 upon binding the transition state analog FK506: Implications for transition state stabilization and target protein recognition. Brath U, Akke M. J. Mol. Biol. 387, 233–244 (2009).

Multiple timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C spin relaxation. Paquin R, Ferrage F, Mulder FAA, Akke M, Bodenhausen G.  J. Am. Chem. Soc. 130, 15805–15807 (2008).

Characterization of Chemical Exchange Using Residual Dipolar Coupling. Igumenova TI, Brath U, Akke M, Palmer AG.  J. Am. Chem. Soc. 129, 13396–13397 (2007).

Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in protein. Lundström P, Teilum K, Carstensen T, Bezsonova I, Wiesner S, Hansen F, Religa TL, Akke M, Kay LE. J. Biomol. NMR 38, 199–212 (2007).

The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G, and RF3 via a conserved region of the L12 C-terminal domain. Helgstrand M, Mandava CS, Mulder FAA, Liljas A, Sanyal S, Akke M. J. Mol. Biol. 365, 468–479 (2007). 

Page Manager: Bertil Halle
Webmaster: webmaster@lth.se
Last updated: 2014-03-17