Related Experiment Video
Updated: Jul 14, 2026

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
Published on: January 31, 2019
Self-organization of guanosine 5'-monophosphate on mica
Klemen Kunstelj1, Francesco Federiconi, Lea Spindler
1Jozef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia. klemen.kunstelj@ijs.si
Abstract:
Self-assembled aggregates of guanosine 5'-monophosphate (GMP) on the surface of muscovite mica were investigated by atomic force microscopy (AFM). Aqueous solutions of sodium, potassium and ammonium GMP salts were studied. For solution concentrations c < 0.005 wt% only small islands of deposited material are present on the surface. For c approximately 0.02 wt%, in addition to the islands and patches, also linear aggregates called G-wires are formed. The wire-like aggregates are on average 1.9 nm high and can be several micrometers long. They exhibit a profound directional growth along the six main crystallographic axes of the basal plane of mica. For c > 0.1 wt% flat terraces with the height of 2.5 nm appear. They are formed of G-wires lying with their long axis parallel to the substrate and stacking in a hexagonal arrangement. The morphology of the adsorbates is independent of the type of salt used to prepare the initial solution. This signifies that intrinsic potassium ions from the substrate play much more important role in the GMP adsorption than cations from the solution.
Related Concept Videos
GTPases and their Regulation
Large G-proteins, also known...
GTPases and their Regulation
Large G-proteins, also known...
Activation and Inactivation of G Proteins
IP3/DAG Signaling Pathway
Coat Assembly and GTPases
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:

