Beta-carbonic anhydrase molecule F006 / 9286
Wall Art and Photo Gifts from Science Photo Library
Beta-carbonic anhydrase molecule F006 / 9286
Beta-carbonic anhydrase, molecular model. This enzyme is from the red algae Porphyridium purpureum. It catalyses the reversible hydration of carbon dioxide
Science Photo Library features Science and Medical images including photos and illustrations
Media ID 9253503
© LAGUNA DESIGN/SCIENCE PHOTO LIBRARY
Alga Algae Alpha Helix Beta Sheet Enzyme Proteomics Red Algae Strand Tertiary Structure Biochemical Biochemistry Cutouts Molecular Molecular Model Molecular Structure Protein
EDITORS COMMENTS
This print showcases the intricate molecular structure of Beta-carbonic anhydrase, a vital enzyme found in red algae known as Porphyridium purpureum. The white background beautifully contrasts with the vibrant illustration, allowing for a clear focus on this remarkable biological marvel. Within the image, one can observe the detailed arrangement of alpha helices and beta sheets that form the tertiary structure of this protein molecule. This molecular model represents years of research and serves as a valuable tool in various fields such as biology, medicine, and biochemistry. The primary function of Beta-carbonic anhydrase is to facilitate the reversible hydration process of carbon dioxide. Its catalytic abilities play a crucial role in maintaining equilibrium within living organisms by regulating pH levels and aiding in metabolic processes. This stunning artwork not only highlights the beauty inherent in nature's microscopic wonders but also emphasizes its significance within healthcare and medical research. The cutout design further enhances our understanding by providing a three-dimensional perspective on this essential enzyme. Created by LAGUNA DESIGN/SCIENCE PHOTO LIBRARY, this print offers both scientific accuracy and aesthetic appeal. It serves as a testament to human curiosity and dedication towards unraveling the mysteries hidden within even seemingly simple organisms like red algae.
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