ライフサイエンスコーパス: association state

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1 roenvironments in response to changes in its association state.

2 nd 3 without significantly altering its self-association state.

3 s responsible for the observed difference in association state.

4 ntermembrane junctions and find two distinct association states.

5 al studies have been performed regarding its association state and biological/structural stability.

6 iologic mechanisms may alter the native self-association state and contribute to apoA-I dysfunction.

7 ype enzyme in secondary structure or subunit association state, as shown by circular dichroism spectr

8 rations of denaturants show no change in the association state before the unfolding transition and ar

9 ittin, corresponding to two melittin-bilayer association states, could be used to interpret the exper

10 otides and related the binding properties to association states determined from sedimentation propert

11 oth the amphiphilic environment and the self-association state of CcO affect its kinetic stability.

12 SAXS and SEC-HPLC results indicate that the association state of DnaK is very sensitive to the buffe

13 The association state of FliN in solution was studied by ana

14 These findings about the association state of free L chains are independent of th

15 s of hDlg interactions, we examined the self-association state of full-length hDlg as well as defined

16 Further evaluation of the self-association state of hDlg using sedimentation equilibriu

17 44' and His 55 and Thr 67' do not change the association state of the dimer.

18 l content and by consolidating the monomeric association state of the full-length protein.

19 owever, EGF stimulation had no effect on the association state of the Grb2-SOS or the Nck-SOS complex

20 ny of the uncertainty sources (the solvation/association state of the guest in solution, deviations i

21 This is not related to a change in association state of the polypeptide.

22 In this study, we characterized the self-association states of ExsC, ExsD, and ExsE and the bindi

23 Characterizing the association states of proteins during folding is critica

24 re, SiMPull can distinguish between multiple association states of the same protein.

25 erived neurotrophic factor, and the solution association states of these molecules.

26 To study the association states of unfolded, folded, and intermediate

27 this experiment can be used to determine the association states of unfolded, folded, and kinetic inte

28 within adherens cell-cell junctions, but its association state outside these clusters is unknown.

29 concentrations of urea on the conformation, association state, stability, and kinetics of fibrillati

30 The new Guidelines of the American Heart Association state that lay rescuers can no longer rely o

31 us subtilis NOS loose dimer shows an altered association state with severely destabilized subdomains.

32 tion of insulin involves both changes in the association state (with rate-limiting hexamer dissociati

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