Close correlation of protein thermostability and self-buried area rate revealed by crystal structure of HPr from Thermoanaerobacter tengcongensis MB4 Descriptor: Phosphotransferase system, HPr-related
The kinetic were acquired in vitro with purified proteins. The Tm and m values (indicating the cooperativity of unfolding) were extracted from heat denaturation. N.D.; not determined. Errors shown are
Protein folding is governed by a variety of molecular forces including hydrophobic and ionic interactions. Less is known about the molecular determinants of protein stability. Here we used a recently