Chaperone-Client Interactions: Molecular Mechanisms and Functional Implications

Related lectures (32)

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

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

Explores enzymes, evolution, lipids, membranes, carbohydrates, membrane proteins, and enzyme inhibition mechanisms.

Covers the early classification of organelles in two major intracellular transport pathways and the transfer of lipids between cellular compartments.

Delves into Cryo-EM's role in studying Parkinson's Disease and protein structures at the nano-level.

Discusses the self-attraction of DNA and its mediated interactions.

Explores protein folding dynamics, focusing on chaperone-assisted non-equilibrium stabilization and its implications for biophysics and evolution.

Explores different types of directed motion in cellular systems, emphasizing the role of motor proteins in transporting biomolecules.

Covers protein folding, maturation, degradation, and the implications of misfolding in neurodegenerative diseases.

Delves into protein co-evolution analysis, covering discoveries, residue contacts, and direct coupling analysis.

Explains protein synthesis, translation, and the central dogma of molecular biology.

Explores chaperone-mediated disaggregation of amyloid fibrils by Hsp70 in neurodegenerative diseases.

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