Human ’A-crystallin forms structures of 12, 16 and 20 subunits (from left to right). Two subunits (center, dark and light gray) form a dimer. Image: C. Kaiser / TUM
Human 'A-crystallin forms structures of 12, 16 and 20 subunits ( from left to right ). Two subunits (center, dark and light gray) form a dimer. Image: C. Kaiser / TUM Protective protein in the eye lens affects protein oxidation The lens of the human eye comprises a highly concentrated protein solution, which lends the lens its great refractive power. Protective proteins prevent these proteins from clumping together throughout a lifetime. A team of scientists from the Technical University of Munich (TUM) has now uncovered the precise structure of the 'A-crystallin protein and, in the process, discovered an important additional function. The refractive power of the human eye lens stems from a highly concentrated protein solution. These proteins are created during embryonic development and must then function for a whole life, as the lens has no machinery to synthesize or degrade proteins.
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