Protein Engineering, Vol 11, 753-760, Copyright © 1998 by Oxford University Press
AM Facchiano, G Colonna and R Ragone
We have compared the X-ray structures of 13 thermophilic proteins with
their mesophilic homologues, in order to bring out differences in the
stability of helices. The energy terms of a helix-coil transition algorithm
were used to evaluate helix stability. Helices of thermophilic proteins are
more stable than the mesophilic homologues in 69% of cases. This is due
mainly to intrinsic helical propensities of amino acids, whereas minor
effects are linked to main chain H-bonds, side chain-side chain
interactions, capping motifs and charge-dipole effects. Furthermore, the
frequency of 10 helix stabilizing factors recognized by appropriate
sequence patterns was evaluated. The only factor occurring significantly in
the thermostable proteins was the lack of beta branched residues. Other
factors do not show a definite trend, although their occurrence in proteins
is believed to be important for stability. This is discussed in the light
of protein engineering applications.
ARTICLES
Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study
CRISCEB, Research Center of Computational and Biotechnological Sciences, Naples, Italy.
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