Pepsin molecule

Wall Art and Photo Gifts from Science Photo Library

Pepsin molecule

Pepsin enzyme. Computer graphic of the protein- digesting enzyme pepsin. It is a protease enzyme that is secreted as part of gastric juice into the stomach in an inactive form known as pepsinogen. When it comes into contact with hydrochloric acid it is converted into the active form that hydrolyses proteins into smaller polypeptides (peptones). The molecules backbone (red ribbon) and individual atoms (coloured dots) are seen

Science Photo Library features Science and Medical images including photos and illustrations

Media ID 6274388

© DR TIM EVANS/SCIENCE PHOTO LIBRARY

Atom Atoms Back Bone Catalyst Compound Compounds Digestion Digestive Enzyme Enzymes Graphic Molecules Organic Pepsin Proteomics Structural Bio Chemistry Biochemical Computer Artwork Molecular Protein

EDITORS COMMENTS
This print showcases the intricate structure of a pepsin molecule, an enzyme responsible for protein digestion. Created through computer graphics, this illustration vividly depicts the complex nature of this protease enzyme. Normally secreted as an inactive form called pepsinogen into the stomach as part of gastric juice, it is only when exposed to hydrochloric acid that it transforms into its active state. In this activated form, pepsin hydrolyses proteins into smaller polypeptides known as peptones. The image allows us to explore the molecular composition of pepsin in great detail. The red ribbon represents the backbone of the molecule while colored dots symbolize individual atoms forming its structure. This visual representation offers valuable insights into biochemistry and proteomics by highlighting how enzymes like pepsin act as catalysts in biochemical reactions. Science Photo Library has expertly captured this remarkable artwork that combines scientific precision with artistic flair. It serves not only as a testament to human knowledge and understanding but also provides inspiration for further research in chemistry and molecular biology.

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