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Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL.
Yifrach O, Horovitz A. Yifrach O, et al. Biochemistry. 1998 May 19;37(20):7083-8. doi: 10.1021/bi980370o. Biochemistry. 1998. PMID: 9585518
The results in this study are found to be consistent with the nested model for cooperativity in ATP binding by GroEL [Yifrach, O., and Horovitz, A. (1995) Biochemistry 34, 5303-5308]....
The results in this study are found to be consistent with the nested model for cooperativity in ATP binding by GroEL [Yifrach, O …
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.
Yifrach O, Horovitz A. Yifrach O, et al. Biochemistry. 1995 Apr 25;34(16):5303-8. doi: 10.1021/bi00016a001. Biochemistry. 1995. PMID: 7727391
Two allosteric transitions were previously observed also in the case of the Arg-196-->Ala GroEL mutant [Yifrach, O., & Horovitz, A. (1994) J. Mol. Biol. 243, 397-401]. On the basis of these observations a mathematical model for nested cooperativity in ATP hyd …
Two allosteric transitions were previously observed also in the case of the Arg-196-->Ala GroEL mutant [Yifrach, O., & …
Review: allostery in chaperonins.
Horovitz A, Fridmann Y, Kafri G, Yifrach O. Horovitz A, et al. Among authors: yifrach o. J Struct Biol. 2001 Aug;135(2):104-14. doi: 10.1006/jsbi.2001.4377. J Struct Biol. 2001. PMID: 11580260 Review.
40 results