Large Flexibility of Dihydrofolate Reductase as Revealed by Temperature Effects on the Volume and Compressibility
The partial specific volume and adiabatic compressibility of dihydrofolate reductase (DHFR) from <I>Escherichia coli</I> remarkably increased as temperature was higher, corresponding to the conformational changes as revealed by spectroscopic measurements. These results demonstrate that this protein has a highly flexible structure at the native state whose tertiary structure or hydrophobic core is easily expanded with temperature to produce the internal cavities.
- Chemistry letters
Chemistry letters 1999(6), 507-508, 1999-06-05
The Chemical Society of Japan