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1 leucine in vitro) to form the active ClpP1P2 tetradecamer.
2 o promote a conformation that stabilizes the tetradecamer.
3 much higher oligomer, possibly an intriguing tetradecamer.
4 stigated and compared with that of the GroEL tetradecamer.
5 l monomers and heptameric rings in the GroEL tetradecamer.
6 for viability and together form the ClpP1P2 tetradecamer.
7 ichiometry of 2 mol of DHFR per mol of GroEL tetradecamer.
8 agonist to stabilize assembly of the active tetradecamer.
9 42 displays additional peaks at nonamers and tetradecamers.
10 self-assemble into catalytically active homo-tetradecamers able to cleave small peptides, the Mycobac
11 isoforms, their structural organization into tetradecamers, and their interactions with the unique bi
12 Compact heptamers from the charge-reduced tetradecamer are clearly distinguished from other overla
14 and causing an unprecedented GS dodecamer-to-tetradecamer conversion, which concomitantly deactivates
15 s, as manifested by the GroEL data where the tetradecamer dissociates into heptamers, reflecting the
16 the effect on the conformation of the GroEL tetradecamer, has been examined by electron microscopy.
17 he presence of MgATP, the beta subunits form tetradecamers in a cooperative reaction that is potentia
18 icroscopy averaging, we found that BPH forms tetradecamers in solution, unlike the dodecamers seen in
19 o induce the dissociation of ClpP1 and ClpP2 tetradecamers into heptameric rings, which then re-assoc
21 ns show that disassembly of the native GroEL tetradecamer occurs at the same rate as unfolding of the
22 tron micrographs of ClpAP that show a single tetradecamer of ClpP associated with either one or two C
25 and ab initio quantum simulations on a B-DNA tetradecamer reveal activated reaction pathways that dep
27 hate)) induces conformational changes in the tetradecamer that are independent of the presence of the
28 iation, which can be reassembled back to the tetradecamer, the pressure-dissociated monomers do not r
29 nterface between the two rings formed stable tetradecamers under oxidizing conditions but spontaneous
30 hiometry of 4-5 mol of DHFR per mol of GroEL tetradecamer, while murine DHFR binds to GroEL with a st
31 mplex through loops at their bases to form a tetradecamer with 72 symmetry and a spherical cage-like
32 of an intermediate that was identified as a tetradecamer with the apical and intermediate domains un
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