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Chaperon mechanism

Papp E, Csermely P (2006) Chemical chaperones mechanisms of action and potential use. Handb. Exp. Pharmacol. 172 405-l 6... [Pg.1019]

The effect of adding Kr might be expected to be very similar to that of Ar addition because the ability of Kr to bind O2 and quench 02(a nj is very similar. The expectation that the chaperone mechanism would be important is indeed realized because an increase in Kr partial pressure decreases EF(66) at all investigated. However, the increase in EF(66) with for > 15.5 eV cannot be attributed solely... [Pg.181]

Getting newly synthesized proteins into shape. Cell 101, 119-122. A good summary of chaperone mechanisms. [Pg.154]

Another interesting result obtained in experiments on these ratios of rate constants is the lack of the dependence of the ratio on the nature of the gas collisionally deactivating the vibrationally excited ozone isotopomer [46]. Different mechanisms have been postulated for the collisional deactivation, including the energy transfer mechanism used here and most commonly used elsewhere, and a chaperon mechanism in which the third-body collision partner forms collision complex with the Q or with the Q2 prior to the recombination step. Recently the chaperon mechanism was revisited for ozone formation, analyzing pressure and temperature dependent data on the recombination rate [47]. Since the ratios of rate... [Pg.17]

In rare cases [7],[8] a different mechanism has been identified in neutral association reactions, named the radical-complex (RC) or chaperon mechanism. It involves complexes AM and proceeds by the steps... [Pg.402]

The first step is formation of a long-lived excited complex and the seeond is stabilization by energy transfer. A modification of this mechanism is the Chaperon mechanism,... [Pg.444]

We have studied termolecular collisions between a benzene molecule and two Ar atoms as a function of pressure, temperature and intermolecular potential without presupposing a given mechWsm but, instead, letting the calculations dictate the final results [31]. The results show that termolecular collisions form termolecular complexes and occur by three mechanisms a) the Chaperon mechanism, in which the first Ar in is the first Ar out of the termolecular complex, is the dominant one at high pressures. Two thirds of all termolecular collisions go by this mechanism, b) The Energy Transfer mechanism, in which the first Ar in is the last Ar out of the termolecular complex,... [Pg.444]

Surprisingly, the simple dissociation of diatomic molecules and the reverse recombination process is far from understood. Apparently three different effects are important complex formation (the chaperone mechanism), the... [Pg.155]

This study was conducted only with helium as a buffer gas in order to avoid possible problems resulting from a chaperone mechanism, which could be possible in argon or nitrogen. The behaviour of the third-order rate coefficient, which exhibits a strong negative temperature dependence... [Pg.108]

How does the GroEL-GroES complex function as a chaperone to assist protein folding Although several aspects of the mechanism are not clear, the main features of the functional cycle are known. The first step is the... [Pg.102]

Chaperones bind to exposed hydrophobic surfaces of polypeptide substrates, and through either ATP-dependent or ATP-independent mechanisms facilitate the folding/assembly, intracellular transport, degradation, and activity of polypeptides. [Pg.347]

Figure 2 The classical activation pathway of SHR. SHRs (gray circle) are associated with chaperones (rectangles). After binding of steroid hormones (black circle) SHRs activate target genes in the nucleus. Additional regulation mechanisms, e.g., phosphorylation are described in the text. Figure 2 The classical activation pathway of SHR. SHRs (gray circle) are associated with chaperones (rectangles). After binding of steroid hormones (black circle) SHRs activate target genes in the nucleus. Additional regulation mechanisms, e.g., phosphorylation are described in the text.
Once in the ER lumen, proteins oligomerize and fold. Proper folding in most cases is facilitated by various isomerases and chaperones resident in the ER. Complex mechanisms exist within the ER to ensure that proteins... [Pg.144]


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See also in sourсe #XX -- [ Pg.376 ]




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Chaperones

Chaperons

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