Chaperonin transition from open to closed conformation Chaperonin transition from open to closed conformation
Posted by: batch303

Video duration: 20 seconds
Global video hits: 156

Octamer molecule, a TRiC/CCT chaperonin from bos taurus, works similar to camera aperture. (Booth et al., 2008 - http://www.nature.co m/nsmb/journal/vaop/ ncurrent/suppinfo/ns mb.1436_S1.html)

Related: chaperonin, modeling, molecular, state, structure, transition
What are Chaperones and How do They Work? Pande Group What are Chaperones and How do They Work? Pande Group
Posted by: PandeScience

Video duration: 177 seconds
Global video hits: 7655

Folding@Home
folding.stanford. edu

Related: aggregate, chaperone, chaperonin, folding, helper, protein
GroEL R-to-R\" transition (side view) GroEL R-to-R" transition (side view)
Posted by: hyeoncb

Video duration: 30 seconds
Global video hits: 330

GroEL undergoes R to R" state upon ATP hydrolysis.
K and L helices, the "wing" of apical domain, move downward direction, resulting in the formation of K80-D359 salt-bridge.
To reduce the internal strain, the apical domain undergoes 100 degree clockwise rotation.

Related: chaperonin, groel, molecular, nanomachine
GroEL T-to-R transition (top view) GroEL T-to-R transition (top view)
Posted by: hyeoncb

Video duration: 30 seconds
Global video hits: 224

Transition of GroEL, a molecular chaperone, from T to R state upon ATP binding. Apical domain including hydrophobic patch (H, I helices) rotates counter-clockwise.

Related: chaperonin, groel, molecular, nanomachine
GroEL R-to-R\" transition (top view) GroEL R-to-R" transition (top view)
Posted by: hyeoncb

Video duration: 30 seconds
Global video hits: 181

Upon ATP hydrolysis, GroEL changes its structure from R to R" state. The apical domain rotates more than 100 degree in clockwise manner. As a result, the interior volume of GroEL cavity increases.

Related: chaperonin, groel, molecular, nanomachine
GroEL T-to-R transition (side view) GroEL T-to-R transition (side view)
Posted by: hyeoncb

Video duration: 30 seconds
Global video hits: 131

Salt bridge (K80-E386) switches to R197-E386 upon ATP binding

Related: chaperonin, groel, molecular, nanomachine