File:Dual-Chaperone-Role-of-the-C-Terminal-Propeptide-in-Folding-and-Oligomerization-of-the-Pore-Forming-ppat.1002135.s004.ogv
Summary
Description |
English: Molecular dynamics simulation of proaerolysin F457G. Result of a molecular dynamics simulation of proaerolysin F457G. The secondary structure of every frame, as calculated by the DSSP algorithm, is represented in the cartoon with different colors: yellow is beta sheet; white and cyan are random coil; purple, blue, and red are alpha helix). Mutation F457G, located on the CTP, has a destabilizing effect. Indeed, the CTP loses most of its secondary structure and begins to disconnect from Domain 4. On Domain 4 an unfolding similar to the one observed in the absence of CTP can be detected. The movie was rendered using the VMD software. |
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Source | Video S1 from Iacovache I, Degiacomi M, Pernot L, Ho S, Schiltz M, Dal Peraro M, van der Goot F (2011). "Dual Chaperone Role of the C-Terminal Propeptide in Folding and Oligomerization of the Pore-Forming Toxin Aerolysin". PLOS Pathogens. DOI:10.1371/journal.ppat.1002135. PMID 21779171. PMC: 3136475. | ||
Author | Iacovache I, Degiacomi M, Pernot L, Ho S, Schiltz M, Dal Peraro M, van der Goot F | ||
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Category:Aeromonas hydrophila
Category:Bacterial toxins
Category:CC-BY-2.5
Category:Host-pathogen interactions
Category:Media from PLOS Pathogens
Category:Ogv videos
Category:Pore forming cytotoxic proteins
Category:Precursor proteins
Category:Protein folding
Category:Protein multimerization
Category:Uploaded with Open Access Media Importer
Category:Uploaded with Open Access Media Importer and needing category review
Category:Video display resolution 640 x 480
Category:Videos from open-access scholarly articles
Category:Videos of molecular chaperones
Category:Videos of protein structures
Category:Videos of tertiary protein structure
Category:Videos of transmembrane proteins