Domain-specific chaperone-induced expansion is required for beta-actin folding: a comparison of beta-actin conformations upon interactions with GroEL and tail-less complex polypeptide 1 ring complex (TRiC).
Villebeck L, Moparthi SB, Lindgren M, Hammarström P, Jonsson BH.
Villebeck L, et al. Among authors: lindgren m.
Biochemistry. 2007 Nov 6;46(44):12639-47. doi: 10.1021/bi700658n. Epub 2007 Oct 16.
Biochemistry. 2007.
PMID: 17939680
The action of GroEL on bound flourescein-labeled beta-actin was characterized, and the structural rearrangement was compared to the case of the beta-actin-TRiC complex, employing the homo fluorescence resonance energy transfer methodology previously used [Villebeck, L., Persson, …
The action of GroEL on bound flourescein-labeled beta-actin was characterized, and the structural rearrangement was compared to the case of …