ATPase molecule F006 / 9441
Wall Art and Photo Gifts from Science Photo Library
ATPase molecule F006 / 9441
ATPase molecule. Molecular model of the ATP-dependent oligomerisation domain of N-ethylmaleimide sensitive factor (NSF), a hexameric ATPase. This enzyme is involved in the membrane fusion of vesicles during transport from one cellular compartment to another
Science Photo Library features Science and Medical images including photos and illustrations
Media ID 9254935
© LAGUNA DESIGN/SCIENCE PHOTO LIBRARY
Alpha Helix Atpase Beta Sheet Enzyme Hexamer Hexameric Proteomics Strand Tertiary Structure Biochemical Biochemistry Cutouts Molecular Molecular Model Molecular Structure Protein
EDITORS COMMENTS
This print showcases the intricate ATPase molecule F006/9441, a vital component in cellular transport and membrane fusion processes. The molecular model depicted here represents the ATP-dependent oligomerisation domain of N-ethylmaleimide sensitive factor (NSF), which functions as a hexameric ATPase enzyme. The white background beautifully highlights the detailed illustration, making it an ideal addition to any biology or medical research setting. With its cut-out design, this artwork provides a clear view of the molecular structure, allowing scientists and researchers to delve into its complexity. The NSF molecule is composed of alpha helices and beta sheets that form its tertiary structure. As a hexamer, it consists of six subunits working together harmoniously to carry out its crucial role in vesicle fusion during cellular compartmental transport. This image holds great significance in proteomics and biochemistry studies, providing valuable insights into the functioning mechanisms of enzymes like ATPases. Its presence in healthcare settings further emphasizes its relevance to medical research and advancements. Created by LAGUNA DESIGN for Science Photo Library, this stunning print serves as both an educational tool and an aesthetic piece for those passionate about unraveling the mysteries within biological systems.
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