denatured protein binding

Definition

Target type: molecularfunction

Binding to a denatured protein. [GOC:mlg]

Denatured protein binding describes the interaction of a protein with another protein that has lost its native three-dimensional structure, often due to exposure to heat, chemicals, or extreme pH. This process can occur through various mechanisms, including hydrophobic interactions, electrostatic interactions, and hydrogen bonding. Denatured proteins often expose hydrophobic residues that were previously buried within the folded structure, making them more accessible for binding. This binding can have a variety of consequences, including:

* **Aggregation:** Denatured proteins can aggregate with each other, forming large, insoluble clumps that can disrupt cellular processes.
* **Proteolysis:** Denatured proteins can be more susceptible to proteolysis, which can lead to the degradation of the protein and the loss of its function.
* **Chaperone binding:** Molecular chaperones can bind to denatured proteins, helping to refold them into their native conformations or to target them for degradation.
* **Signal transduction:** Denatured proteins can sometimes act as signals for cellular stress responses, triggering the activation of specific signaling pathways.

The specific consequences of denatured protein binding depend on the nature of the interacting proteins and the cellular context. However, in general, this process can have significant implications for cellular function and homeostasis.'
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Proteins (1)

Compounds (4)