Movie Gallery - Protein Folding and Stretching
All movies and images were made using VMD. Download movie files via the movie file type (.mpg, .mov) after the movie title (right-click in Windows; control-click on Macs). To view original movie files, you may need to try the Quicktime or VLC movie players. You may wish to also visit TCBG's YouTube movie gallery to view science movies. All movies are copyrighted by TCBG.
Six Microseconds of Protein Folding (.mpg, 10.4M) | |||||
Proteins, made of chains of amino acids, carry out most cell functions, once folded into the proper structure. The movie starts with the final crystal structure of the villin protein (colors blue, white, red show different sequences in the protein), and then depicts how villin folds into its final structure over six microseconds. | |||||
A Molecular Flow Sensor Which Induces Blood Clotting (.mpg, 4.8M) | |||||
The movie shows how a peptide chain (in white) connected to a larger protein (via atoms depicted in gold) changes from a disordered loop state to a hairpin shape in response to increase of blood flow, like from a cut. Areas of the peptide chain extend and rotate (highlighted in purple) to form the hairpin, with hydrogen bonds (in green) completing the transition. Once formed, the hairpin holds platelets in place to promote blood clotting around wounds. | |||||
The Fantastic, Elastic, Muscle Protein (.mpg, 4.4M) | |||||
The movie shows a stretching force being applied to six domains (at top, colored separately) of the muscle protein titin, which provides muscle with its elasticity. Like six knots tied on the same string, the titin domains rupture one-by-one with the application of force, rather than simultaneously. The chart shows the force being applied in piconewtons and the extension of the domains in Angstroms. The results speak to fundamental processes of muscle, and may inform how muscle protein mutations are related to muscular dystrophy. | |||||
Forced Unfolding of Titin Z1Z2 (.mpg, 2.9M) | |||||
This movie shows the forced unfolding of titin Z1Z2. A force of 750pN was applied to the C-terminus of Z2 while the N-terminus of Z1 was held fixed. As the structure unravels, we find that intramolecular beta-strands are broken in sequential fashion. | |||||
Forced Unfolding of the Titin Z1Z2-Telethonin Complex (.mpg, 6.7M) | |||||
This movie shows the forced unfolding of the titin Z1Z2-telethonin complex. A force of 1200pN was applied to both titin Z2 termini, resulting in the detachment of the Z2 domain from telethonin via separation of intermolecular beta strands, followed by the subsequent unraveling of the Ig domain. | |||||
Stretching the Anthrax Toxin-Receptor Complex (.mpg, 4.2M) | |||||
This moving shows stretching the receptor CMG2 away from the anthrax toxin protein PA under neutral conditions. | |||||
Stretching FN-III-1 (.mpg, 2.2M) | |||||
Stretching the extra-cellular matrix protein fibronectin type III1 module. | |||||