Editing S-layer (section)

=== In vitro assembly ===
S-layer proteins have the natural capability to self-assemble into regular monomolecular arrays in solution and at interfaces, such as solid supports, the air-water interface, lipid films, liposomes, emulsomes, nanocapsules, nanoparticles or micro beads.<ref name="Sleytr2014" /><ref name="Sleytr2025" /><ref name="Pum2014">
{{cite journal |vauthors=Pum D, Sleytr UB |date=2014 |title=Reassembly of S-layer proteins |journal=Nanotechnology |volume=25 |issue= 31|page=312001 |doi=10.1088/0957-4484/25/31/312001 |pmid= 25030207|bibcode=2014Nanot..25E2001P |s2cid=39889746 }}</ref><ref name="Schuster2014">{{cite journal |vauthors=Schuster B, Sleytr UB |date=2014 |title=Biomimetic interfaces based on S-layer proteins, lipid membranes and functional biomolecules |url=http://rsif.royalsocietypublishing.org/node/7191.full |journal=J. R. Soc. Interface |volume=11 |issue=96 |page=20140232 |doi=10.1098/rsif.2014.0232 |pmid=24812051 |pmc=4032536 }}</ref> S-layer crystal growth follows a non-classical pathway in which a final refolding step of the S-layer protein is part of the lattice formation.<ref name="Chung2010">{{cite journal |vauthors=Chung S, Shin SH, Bertozzi CR, De Yoreo JJ  |date=2010 |title=Self-catalyzed growth of S layers via an amorphous-to-crystalline transition limited by folding kinetics |journal=Proc. Natl. Acad. Sci. USA |volume=107 |issue=38 |pages=16536–16541 |doi=10.1073/pnas.1008280107 |pmid=20823255 |pmc=2944705 |bibcode=2010PNAS..10716536C |doi-access=free }}</ref><ref name="Shin2012">{{cite journal |vauthors=Shin SH, Chung S, Sanii B, Comolli LR, Bertozzi CR, De Yoreo JJ |date=2012 |title=Direct observation of kinetic traps associated with structural transformations leading to multiple pathways of S-layer assembly |journal=Proc. Natl. Acad. Sci. USA |volume=109 |issue= 32|pages=12968–12973 |doi=10.1073/pnas.1201504109 |pmid=22822216 |pmc=3420203  |bibcode=2012PNAS..10912968S |doi-access=free }}</ref>