Jigsaw Puzzle : Rhinovirus capsid, molecular model F006 / 9490
Jigsaw Puzzles from Science Photo Library
Rhinovirus capsid, molecular model F006 / 9490
Rhinovirus capsid, molecular model. This is human rhinovirus. The rhinovirus infects the upper respiratory tract and is the cause of the common cold. It is spread by coughs and sneezes. In viruses, the capsid is the protein shell that encloses the genetic material. A capsids subunits are capsomeres that self-assemble to form the shell seen here. Here, this shell, approximately spherical in shape, has icosahedral symmetry. One of the functions of the capsid is to aid the transmission of the viral genetic material into host cells. The cell mechanisms are then used to produce new virus particles
Science Photo Library features Science and Medical images including photos and illustrations
Media ID 9255435
© LAGUNA DESIGN/SCIENCE PHOTO LIBRARY
Alpha Helix Beta Sheet Capsid Capsomere Common Cold Icosahedral Illness Infection Microbiology Proteomics Rhinovirus Strand Tertiary Structure Viral Virion Virology Virus Particle Biochemical Biochemistry Cutouts Disorder Microbiological Molecular Molecular Model Molecular Structure Pathogen Protein Virus
Jigsaw Puzzle (500 Pieces)
Discover the intricacies of the natural world with our Media Storehouse Jigsaw Puzzles, featuring the captivating image of a Rhinovirus capsid molecular model (F006 / 9490) from LAGUNA DESIGN/SCIENCE PHOTO LIBRARY. Delve into the microscopic realm and piece together this scientific puzzle, revealing the structure of this common cold-causing virus. Assemble the intricate details of the Rhinovirus capsid and expand your knowledge of virology, one puzzle piece at a time.
500 piece puzzles are custom made in Australia and hand-finished on 100% recycled 1.6mm thick laminated puzzle boards. There is a level of repetition in jigsaw shapes with each matching piece away from its pair. The completed puzzle measures 40x51cm and is delivered packaged in an attractive presentation box specially designed to fit most mail slots with a unique magnetic lid
Jigsaw Puzzles are an ideal gift for any occasion
Estimated Product Size is 40.3cm x 50.7cm (15.9" x 20")
These are individually made so all sizes are approximate
Artwork printed orientated as per the preview above, with landscape (horizontal) or portrait (vertical) orientation to match the source image.
EDITORS COMMENTS
This print showcases a molecular model of the Rhinovirus capsid, providing a glimpse into the intricate structure of this common cold-causing pathogen. The Rhinovirus primarily targets the upper respiratory tract and is transmitted through coughs and sneezes, making it highly contagious. At the core of this image lies the protein shell known as the capsid, which envelops the virus's genetic material. Composed of numerous self-assembling capsomeres, these subunits come together to form an approximately spherical shell with icosahedral symmetry. This symmetrical arrangement aids in transmitting the viral genetic material into host cells during infection. The detailed molecular structure depicted here offers valuable insights for researchers in biology and medicine who strive to understand how viruses function and develop potential treatments or preventive measures against them. By studying elements such as alpha helices, beta sheets, tertiary structures, and other biochemical features present within this model, scientists can unravel key mechanisms behind viral infections. With its white background contrasting against vibrant colors representing different components of the virus particle, this artwork serves as a powerful visual tool for exploring virology and microbiology concepts. It exemplifies how scientific illustrations can bridge gaps between complex research findings and broader audiences interested in healthcare advancements. This print by LAGUNA DESIGN/SCIENCE PHOTO LIBRARY not only captures an intriguing moment at a microscopic level but also highlights our ongoing quest to combat infectious diseases like rhinovirus through cutting-edge research in biochemistry and proteomics.
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