Protein memory research papers
A pathway for conformational diversity in proteins mediated by intramolecular chaperones
Point mutations within IMCs alter folding, resulting in structural conformers that specifically interact with their cognate IMCs in a process termed protein memory. Here, we show a mechanism that mediates conformational diversity in subtilisin.
Biomolecular electronics: protein-based associative processors and volumetric memories
irradiated volume elements. The methods and procedures of prototyping these bioelectronic devices are discussed. We also examine current efforts to optimize the protein memory medium by using chemical and genetic methods.
Future memory storage technology: protein-based memory devices may facilitate surpassing Moore's law
Lipid-assisted protein folding
prior to the involvement of PE. A similar concept of protein memory was used to describe the action of intramolecular chaperones represented by the propeptides of some proteases (50). Subtilisin and a-lytic protease purified
Efficient algorithms for protein-based associative processors and volumetric memories
devices. In addition, bacteriorhodopsin protein memory devices exhibit increased thermal, chemical and photochromic stability, and have the advantage of being portable, radiation-hardened, waterproof, and EMP-resistant.
Chaperoning Anfinsen: the steric foldases
Moreover, subtilisin exemplifies a striking case of 'protein memory' of the protease and emphasizes that steric information is 'imprinted' upon the protease by the propeptide. Protein memory through altered folding mediated by intramolecular chaperones.
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