Stability and folding of ultrastable proteins: eye lens crystalline and enzymes from thermophiles 1

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Abstract
Soluble globular proteins exhibit marginal stabilities, equivalent to only a few weak intermolecular interactions. Extreme conditions in the biosphere, as well as acute physiological stress, require either mutative adaptation or stabilization by accessory proteins or extrinsic factors such as metabolites, cofactors, or compatible solvent components. No general strategies of stabilization have yet been established. However, certain contributions to stability have been elucidated by analyzing extremely stable proteins, such as crystallins from the eye lens, or proteins from hyperthermophilic microorganisms. Relating the structure and stability of homologous proteins from mesophiles and extremophiles, it becomes clear that stability increments may accumulate from 1) local interactions, 2) secondary or supersecondary structure, 3) packing and docking of domains, 4) association of subunits, and 5) conjugation with prosthetic groups, carbohydrate moieties, or nucleic acids, etc. Single and multiple point mutati...

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