Extraordinary Proteins
By adapting their proteins, organisms have managed to colonize extraordinary environments. "Extreme" proteins demonstrate many intriguing biophysical features neccessary for living in harsh environments.
Well-tuned surface charges enable solubility in a broad range of salt conditions
The green alga Dunaliella salina lives in the Dead Sea of Israel where water currents can change its environment swiftly and dramatically from low to high salt concentrations. The problem for its proteins is staying soluble in both solvents.
In 2005, scientists from the Weizmann Institute reported the first crystal structure of a halotolerant enzyme, from D. salina, a (1y7w). In 1995, they solved (together with scientists from Tel Aviv University) the first structure of a halophilic enzyme, a (1hlp) from Haloarcula marismortui.
They conclude that a general solution for remaining soluble in salty conditions is to become "anion-like" through increasing the negative charge surface density. Too little negative charge and the enzyme can only tolerate low salt conditions, too much negative charge and the enzyme can only stand high salt conditions, but the "right" amount of negative charge enables an enzyme to remain soluble in both low and high salt conditoins.
In the list below, notice how the negative surface charge density - the ratio of negative "redish" amino acids to positive "bluish" amino acids - is low for the mesophilic enzymes, high for the halophilic enzymes, and medium for the halotolerant enzyme. These ratios are approximately 1:1 (negative to positive amino acids on the surface) for the mesophilic enzymes; 3:1 for the halophilic enzyme, and 2:1 for the halotolerant enzyme.
