Editing Lysozyme (section)

=== Enzyme conformation changes ===
Lysozyme exhibits two conformations: an open active state and a closed inactive state. The catalytic relevance was examined with single walled [[carbon nanotube]]s (SWCN) field effect transistors (FETs), where a singular lysozyme was bound to the SWCN FET.<ref>{{cite journal | vauthors = Choi Y, Moody IS, Sims PC, Hunt SR, Corso BL, Perez I, Weiss GA, Collins PG | title = Single-molecule lysozyme dynamics monitored by an electronic circuit | journal = Science | volume = 335 | issue = 6066 | pages = 319–324 | date = January 2012 | pmid = 22267809 | pmc = 3914775 | doi = 10.1126/science.1214824 | bibcode = 2012Sci...335..319C }}</ref> Electronically monitoring the lysozyme showed two conformations, an open active site and a closed inactive site. In its active state lysozyme is able to [[Processivity|processively]] hydrolyze its substrate, breaking on average 100 bonds at a rate of 15 per second. In order to bind a new substrate and move from the closed inactive state to the open active state requires two conformation step changes, while inactivation requires one step.{{cn|date=July 2024}}