ライフサイエンスコーパス: tetradecamer

1 agonist to stabilize assembly of the active tetradecamer.

2 o promote a conformation that stabilizes the tetradecamer.

3 stigated and compared with that of the GroEL tetradecamer.

4 l monomers and heptameric rings in the GroEL tetradecamer.

5 leucine in vitro) to form the active ClpP1P2 tetradecamer.

6 ichiometry of 2 mol of DHFR per mol of GroEL tetradecamer.

7 pX hexamer and its interaction with the ClpP tetradecamer.

8 roEL, where the only oligomeric species is a tetradecamer.

9 much higher oligomer, possibly an intriguing tetradecamer.

10 for viability and together form the ClpP1P2 tetradecamer.

11 42 displays additional peaks at nonamers and tetradecamers.

12 self-assemble into catalytically active homo-tetradecamers able to cleave small peptides, the Mycobac

13 isoforms, their structural organization into tetradecamers, and their interactions with the unique bi

14 Compact heptamers from the charge-reduced tetradecamer are clearly distinguished from other overla

15 orce microscopy images are compatible with a tetradecamer but not a trimer.

16 and causing an unprecedented GS dodecamer-to-tetradecamer conversion, which concomitantly deactivates

17 s, as manifested by the GroEL data where the tetradecamer dissociates into heptamers, reflecting the

18 the effect on the conformation of the GroEL tetradecamer, has been examined by electron microscopy.

19 -like assemblies: a dodecamer in Aq880 and a tetradecamer in Hth1307.

20 protein hetero-decamer, a 800 kDa GroEL homo-tetradecamer in its apo-form or loaded with its ATP cofa

21 the fully-formed heptamer and an "inverted" tetradecamer in which the two heptamers associate via th

22 he presence of MgATP, the beta subunits form tetradecamers in a cooperative reaction that is potentia

23 icroscopy averaging, we found that BPH forms tetradecamers in solution, unlike the dodecamers seen in

24 o induce the dissociation of ClpP1 and ClpP2 tetradecamers into heptameric rings, which then re-assoc

25 The hollow interior enclosed by the tetradecamer is lined with hydrophilic residues and has

26 ns show that disassembly of the native GroEL tetradecamer occurs at the same rate as unfolding of the

27 tron micrographs of ClpAP that show a single tetradecamer of ClpP associated with either one or two C

28 ainst oligopeptide substrates (>10,000 min-1/tetradecamer of ClpP).

29 We present here SID of a large noncovalent tetradecamer protein, GroEL (801 kDa).

30 and ab initio quantum simulations on a B-DNA tetradecamer reveal activated reaction pathways that dep

31 Moreover, the chaperonin tetradecamers show a different interring subunit arrange

32 m and characterize the previously unreported tetradecamer state.

33 hate)) induces conformational changes in the tetradecamer that are independent of the presence of the

34 is a part of a heteromeric PaClpP1(7) P2(7) tetradecamer that is required for proper biofilm develop

35 iation, which can be reassembled back to the tetradecamer, the pressure-dissociated monomers do not r

36 action also favors a remarkable dodecamer to tetradecamer transition in some GS, breaking the paradig

37 nterface between the two rings formed stable tetradecamers under oxidizing conditions but spontaneous

38 hiometry of 4-5 mol of DHFR per mol of GroEL tetradecamer, while murine DHFR binds to GroEL with a st

39 mplex through loops at their bases to form a tetradecamer with 72 symmetry and a spherical cage-like

40 of an intermediate that was identified as a tetradecamer with the apical and intermediate domains un