Dissociation Kinetics of the GroEL−gp31 Chaperonin Complex Studied with Förster Resonance Energy Transfer

Biochemistry ◽  
2009 ◽  
Vol 48 (49) ◽  
pp. 11692-11698 ◽  
Author(s):  
Stéphane Calmat ◽  
Johnny Hendriks ◽  
Harm van Heerikhuizen ◽  
Christoph F. Schmidt ◽  
Saskia M. van der Vies ◽  
...  





2009 ◽  
Vol 25 (3) ◽  
pp. 874-881 ◽  
Author(s):  
Mojgan Kavoosi ◽  
A. Louise Creagh ◽  
Robin F. B. Turner ◽  
Douglas G. Kilburn ◽  
Charles A. Haynes


2015 ◽  
Vol 3 (45) ◽  
pp. 8865-8873 ◽  
Author(s):  
Dahai Yu ◽  
Guangyang Zou ◽  
Xiaojing Cui ◽  
Zhengwei Mao ◽  
Irina Estrela-Lopis ◽  
...  

The FRET technique was used to quantify the surface cleavage kinetics of PLGA particles containing disulfide bonds in cells.



2002 ◽  
Vol 30 (2) ◽  
pp. 55-61 ◽  
Author(s):  
K. Török

The conformation of Ca2+/calmodulin changes from extended when free in solution to compact when bound in peptide complexes. The extent and kinetics of calmodulin compaction in association with Ca2+/calmodulin-dependent protein kinases (CaMKs), as well as target peptides, were investigated by fluorescence, resonance energy transfer and stopped-flow kinetics. Compaction of Ca2+/ calmodulin labelled with resonance energy-transfer probes in association with target peptides was rapid (>350 s−1). With the target enzymes smooth-muscle myosin light-chain kinase, CaMKIV and αcCaMKII, the rates of calmodulin compaction were one-two orders of magnitude lower compared with those of the peptides and in the case of αCaMKII, ATP binding and Thr286 auto-phosphorylation were required for calmodulin compaction. In the absence of nucleotides, Ca2+/calmodulin bound to αCaMKII in extended conformations, initially probably attached by one lobe only. Kinetic data suggest that in the activation process of Ca2+/ calmodulin-dependent protein kinases, productive as well as unproductive complexes are formed. The formation of productive complexes with Ca2+/calmodulin thus may determine the rate of activation.







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