Revisiting the correlation between proteins' thermoresistance and organisms' thermophilicity

Yves Dehouck, Benjamin Folch, Marianne Rooman
2008 Protein Engineering Design & Selection  
The possibility to rationally design protein mutants that remain structured and active at high temperatures strongly depends on a better understanding of the mechanisms of protein thermostability. Studies devoted to this issue often rely on the living temperature (T env ) of the host organism rather than on the melting temperature (T m ) of the analyzed protein. To investigate the scale of this approximation, we probed the relationship between T m and T env on a dataset of 127 proteins, and
more » ... 7 proteins, and found a much weaker correlation than previously expected: the correlation coefficient is equal to 0.59 and the regression line is T m 42.98 8 8 8 8C 1 0.62T env . To illustrate the effect of using T env rather than T m to analyze protein thermoresistance, we derive statistical distance potentials, describing Glu -Arg and Asp -Arg salt bridges, from protein structure sets with high or low T m or T env . The results show that the more favorable nature of salt bridges, relative to other interactions, at high temperatures is more clear-cut when defining thermoresistance in terms of T m . The T envbased sets nevertheless remain informative.
doi:10.1093/protein/gzn001 pmid:18245807 fatcat:3w2ne6fxkvaergdugzhg74gjwq