Only 15 years ago macromolecular crowding was still underappreciated. The last years have seen an increasing relevant number of crowding-regulated mechanisms coming to light; as the regulation of gene expression, the gating energies of membrane proteins or the regulation of the membrane protein conformational landscape.
The cell membrane is crowded with proteins, protein content reaches area fractions of 0.55 and even crystalline densities in extreme cases.
High Speed Atomic Force Microsocopy has brought new possibilities to study macromolecular crowding in membranes, providing location and structural information on unlabelled molecules with sub-second temporal resolution and full visualization of the local crowding of the molecular nanoenvironment.
‘Lysenin toxin membrane insertion is pH-dependent and non-cooperative´ Munguira, I. Casuso (co-first autor), H. Takahashi, S. Scheuring 2017 Biophysical J 113(9), 2029-2036 (IF: 3.6)´
´Glasslike Membrane Protein Diffusion in a Crowded Membrane´ I. Munguira, I. Casuso (co-first autor), H. Takahashi, F. Rico, A. Miyagi, M. Chami, S. Scheuring 2016 ACS nano 10 (2), 2584-2590 (IF: 12.8)
´Characterization of the motion of membrane proteins using high-speed atomic force microscopy´ I. Casuso, J. Khao, M. Chami, P. Paul-Gilloteaux, M. Husain, JP. Duneau, H. Stahlberg, JN. Sturgis, S.Scheuring 2012 Nature nanotechnology 7 (8), 525-529 (IF: 34.0)
Diffusion of a crowded ensemble of OmpF trimers by HS-AFM on TV