The shear induced membrane folding was not described in literature before, but besides microcapsules it could also be observed for flat membranes.
Membrane folds were not seen beneath osteoclasts incubated on vitronectin-coated substrates in the presence of calcitonin.
The membrane folds are held in place by structures called cristae junctions, which may also help to restrict proteins to particular areas of the inner membrane.
Membrane protein folding is complicated by the need to recreate a suitable membrane mimetic environment in vitro into which the protein can fold [47].
An important feature of alpha helical membrane protein folding is protein topology, which can be either single-span or multi-span, represented by the parameter kProt [54].
By contrast, the experimental toolbox for the study of membrane protein folding is more limited [141].
Recent trends, however, suggest that the field of membrane protein folding is already progressing towards more complex folding systems.
Finding experimental conditions under which membrane protein folding is fully reversible and reaches equilibrium on experimentally tractable timescales in vitro is challenging and continues to impede studies of membrane protein folding and stability [174].
Consequently, mechanistic details and structural information about membrane protein folding are now emerging at an ever increasing pace.
The effects of DMP1-eGFP expression in tobacco and Arabidopsis suggest that DMP1 regulates membrane folding and is involved in tonoplast and ER membrane fusion and fission reactions.
