Credit: SCI-VIS IFC-CNR/SCIENCE PHOTO LIBRARY

Caption: Protein interactions animation. Clip 7 of 10. This clip forms part of an animation sequence showing protein interactions within a dividing cell. This clip, which includes labels, shows a molecule of the protein calmodulin (CaM, calcium-modulated protein) surrounded by ions and other small, fast-moving molecules. It is transiting from an unbound state (ApoCaM) to the state in which it is bound to four calcium ions (CaCaM). This process changes the shape (conformation) of the protein, and is an important step that enables this protein to bind to other proteins. The full sequence of ten clips shows the interaction between CaM, calcium ions, the MLCK (myosin light-chain kinase) protein, and the actin-myosin bundles of the cell's cytoskeleton, resulting in contraction of the membrane and cell division. For the entire sequence, see clips K003/3847 to K003/3838. For the same sequence as an anaglyph 3D animation, see clips K003/4492 to K003/4483.

Release details: Model release not required. Property release not required.

Keywords: animated, animation, apocam, binding, biochemical, biochemistry, biological, biology of cells, black-and-white, bound, cacam, calcium ions, calcium-modulated protein, calmodulin, cam, cell biology, cellular, changing shape, cnr, computer model, conformation, cytokinesis, cytology, cytoskeleton, interactions, ion, ions, labelled, labels, macromolecule, modelled, molecular, molecule, molecules, monochrome, nanoscale, protein, protein interaction, protein shape, proteins, research, scientific visualization unit, scivis, sequence, series, simulated, simulation

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Protein interactions, bound calmodulin

K003/3841 Rights Managed

Downloadable master

Duration: 00:00:05.12

Frame size: 1280x720

Frame rate: 25

Audio: No

Format: QuickTime, Photo JPEG 100%, progressive scan, square pixels

File size: 42.5M

Original

Capture format: QuickTime Animation

Codec: Photo - JPEG

Please contact Science Photo Library if you require the original, or other formats.

 

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