Hsp70 Molecular Chaperones: Conformational Flexibility and Function

Related lectures (31)

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Series explores computational protein design, covering challenges, applications, and importance in bioengineering and synthetic biology.

Explores chaperones' role in guiding protein folding and preventing misfolding through the functional cycle of Hsp70 and the DnaK chaperone system.

Explores Hsp70's role in protein unfolding and entropic pulling, discussing chaperone-driven stabilization and ATP hydrolysis.

Explores protein dynamics, focusing on ClpB machinery, fast conformational changes, and substrate translocation mechanisms.

Delves into non-refoldability in the E. coli proteome, exploring protein folding challenges and implications.

Explores glass and melting transitions in polymers, including characterization methods and specific polymer properties.

Explores high-speed protein observations, time-resolved methods, cryo-EM, melting dynamics, and future outlooks.

Explores fundamental thermodynamics concepts, laws, energy transfer, and system analysis.

Explores the chaperone mechanism of Grp94 in ER protein quality control and client protein activation.

Explores the molecular mechanism and client preference of chaperonin GroEL in protein folding and aggregation prevention.