This facilitates the identification of changes in structural features that helps render the protein stableunder its particular native physiological conditions.
Thermodynamics analysis reveals that the of marginal stability between the native versusdenatured state extends to proteins isolated from such extreme environments.
It might be expected that proteins isolated from thermophiles and hyperthermophiles would exhibitan increased level of intramolecular stabilizing interactions, in order to compensate for thedestabilizing influence of elevated temperature.
Conversely, it could be predicted that, in order to remain at appropriate degree of conformationalflexibility, proteins from psychrophiles would display decreased levels of such stabilizinginteractions.
Increased thermal stability is generally related to one or more of the following structural adaptations:
An increase in the number of intramolecular polypeptide hydrogen bonds.
An increase in the number of salt bridges.
Increased polypeptide compactness (improved packing of hydrophobic regions)
Extended helical regions.
Stability of proteins derived from psychrophiles
Enhanced stability/functional flexibility of proteins derived from psychrophiles appear to be achieved byone or more of the following adaptations:
Fewer salt links
Reduced aromatic interactions within the hydrophobic core (reduction in hydrophobicity)
Increased hydrogen bonding between the protein surfaces of the surrounding solvent.
Occurrence of extended surface loops.
Conformational stability of proteins
The stability of a protein, i.e. its usefulness as a biologically active molecule, depends on the particular environment and the exposure to conditions that can promote chemical deterioration or conformationalchanges.
1.in vivo stability
Under in vivo condition, protein stability (turnover) is governed by the action of proteolyticenzymes.3