Chaperonin protein F006 / 9690
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Chaperonin protein F006 / 9690
Chaperonin protein, molecular mode. Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation (clumping) due to mis-folded proteins
Science Photo Library features Science and Medical images including photos and illustrations
Media ID 9257053
© LAGUNA DESIGN/SCIENCE PHOTO LIBRARY
Aggregation Alpha Helix Assistance Beta Sheet Chaperonin Cut Otus Facilitation Icosahedral Molecules Preventing Prevention Proteins Proteomics Tertiary Structure Assisting Biochemical Biochemistry Cutouts Molecular Molecular Model Molecular Structure Protein
EDITORS COMMENTS
This print showcases the intricate molecular structure of Chaperonin protein F006/9690, a vital player in the world of biology and medicine. Against a pristine white background, this stunning illustration provides an insightful glimpse into the fascinating realm of protein folding. Chaperonins are specialized proteins that act as facilitators, creating optimal conditions for other proteins to fold correctly. By preventing aggregation or clumping caused by misfolded proteins, they play a crucial role in maintaining cellular health and function. The detailed molecular model depicted here highlights various elements such as alpha helices and beta sheets that contribute to the tertiary structure of chaperonin protein F006/9690. Its icosahedral shape adds to its unique characteristics, allowing it to efficiently assist in protein folding processes. With applications spanning from research to medicine, this artwork represents the significant impact chaperonins have on healthcare advancements. The cut-out design further emphasizes their importance within proteomics and biochemistry fields. Created by LAGUNA DESIGN/SCIENCE PHOTO LIBRARY, this image serves as a reminder of how these remarkable molecules work tirelessly behind the scenes to ensure proper protein functioning while preventing potential harm caused by misfolding.
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