STRUCTURAL ASPECTS OF PROTEIN THERMOSTABILITY

Basing on literature data, the structural features underlying the diff erences between thermophilic proteins and their mesophilic analogs are summarized. It is shown that thermostabilization in the family of rib osomal proteins L1 can be due to extra alternating charge clusters and clusters of aromatic residues, more stable alpha-helices and beta-she ets, and increased number of good alpha-helix-forming and beta-structu re-forming residues.