Related Experiment Video
Updated: May 9, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
Published on: March 10, 2021
H-bond refinement for electron transfer membrane-bound protein-protein complexes: cytochrome c oxidase and cytochrome
Diego Masone1, Facundo Ciocco Aloia, Mario G Del Pópolo
1Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Ciencias Básicas (ICB), Universidad Nacional de Cuyo (UNCUYO), Argentina.
Abstract:
In this study we propose a protocol to evaluate membrane-bound cytochrome c oxidase-cytochrome c552 docking candidates. An initial rigid docking algorithm generates docking poses of the cytochrome c oxidase-cytochrome c552, candidates are then aggregated into a 512-DPPC membrane model and solvated in explicit solvent. Molecular dynamic simulations are performed to induce conformational changes to membrane-bound protein complexes. Lastly each protein-protein complex is optimized in terms of its hydrogen bond network, evaluated energetically and ranked. The protocol is directly applicable to other membrane-protein complexes, such as protein-ligand systems.
Related Concept Videos
Electron Transport Chain: Complex III and IV
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
The Supercomplexes in the Crista Membrane
Electron Transport Chains
The ETC is comprised of...
Electron Transport Chain Components
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
