Single-molecular pair interactions

Single-molecular interaction studies were initially undertaken to elucidate pairwise interactions of selected sets of biololgical macromolecules. One example is related to determination of the mode of action of the mannuronan C-5 epimerase when catalyzing the conversion of the mannuronic acid to its C-5 epimer, guluronic acid, at the polymer level. Such single-molecule interactions are currently adopted for characterization of other molecular pairs, e.g., selected part of immunlogical signalling cascades (toll-like receptor 9 (TLR9)), mucin - lectin interactions, DNA-repair enzymes and selected high molecular weight polysaccharides forming physical gels.

References:

• Single molecular pair interactions between hydrophobically modified hydroethyl cellulose and amylose determined by dynamic force spectroscopy.
  Takemasa, M., Sletmoen, M., and Stokke, B.T.
  Langmuir 25 (2009) 10174-10182
• Single-molecule pair unbinding studies of the soybean agglutinin and the α-GalNAc (Tn-antigen) form of porcine submaxillary mucin.
  Sletmoen, M., Dam, T.K., Gerken, T A., Stokke, B.T., and Brewer, C. F.
  Biopolymers 91 (2009) 719-728.
• Macromolecular motion at the nanoscale of enzymes working on polysaccharides.
  Sletmoen, M., Bræk G.S., and Stokke, B.T.
  Lecture Notes in Physics 711 (2007) 161-180.
• Mapping enzymatic functionalities of mannuroan C-5-epimerases and their modular units by dynamic force spectroscopy.
  Sletmoen, M., Skjåk-Bræk, G. and Stokke, B.T.
  Carbohydr. Res. 340 (2005) 2782-2795.
• Single-molecular pair unbinding studies of mannuronan C-5 epimerase AlgE4 and its polymer substrate.
  Sletmoen, M., Skjåk-Bræk, G. and Stokke, B.T.
  Biomacromolecules 5 (2004) 1288-1295.