Unpicking allosteric mechanisms of homo-oligomeric proteins by determining their successive ligand binding constants
2018 ◽
Vol 373
(1749)
◽
pp. 20170176
◽
Keyword(s):
Advances in native mass spectrometry and single-molecule techniques have made it possible in recent years to determine the values of successive ligand binding constants for large multi-subunit proteins. Given these values, it is possible to distinguish between different allosteric mechanisms and, thus, obtain insights into how various bio-molecular machines work. Here, we describe for ring-shaped homo-oligomers, in particular, how the relationship between the values of successive ligand binding constants is diagnostic for concerted, sequential and probabilistic allosteric mechanisms. This article is part of a discussion meeting issue ‘Allostery and molecular machines’.
2019 ◽
Vol 20
(20)
◽
pp. 5181
◽
2009 ◽
Vol 22
(4)
◽
pp. 319-329
◽
2015 ◽
Vol 34
◽
pp. 7-16
◽
2017 ◽
Vol 420
◽
pp. 43-50
◽
2014 ◽
Vol 25
(7)
◽
pp. 1305-1305
2004 ◽
Vol 15
(3)
◽
pp. 388-397
◽
2012 ◽
Vol 23
(10)
◽
pp. 1768-1777
◽