Structure Elucidation of the clCry4 C-terminal Domain and its Light-induced Conformational Dynamics by single molecule Fluorescence Resonance Energy Transfer (smFRET)

Not scheduled
20m

Description

Cryptochrome (CRY) is a uniquely distinctive member of the photosensitive flavoprotein family, performing diverse functions across different species. At the beginning of this century, it was boldly proposed as a biological magnetoreceptor protein involved in geomagnetic navigation. Subsequent experimental evidence has increasingly supported this prediction. Magnetoreception represents one of the most enigmatic senses in biology, providing migratory animals with directional navigation capabilities, yet its molecular mechanisms remain largely unresolved. As a candidate magnetoreceptor molecule, cryptochrome‘s working mechanism involves quantum effects of photoinduced radical pairs (Radical Pair Mechanism, RPM). In recent years, the radical pair-based magnetoreception hypothesis has gained theoretical and experimental support. However, crucial molecular-level evidence, particularly direct observation and validation of how magnetic fields influence protein conformation, remains lacking.

Primary author

Presentation materials