TAILIEUCHUNG - Báo cáo khoa học: Protein hyperthermostability – current status and beyond Sotirios Koutsopoulos

The discovery of hyperthermophilic microorganisms, thriv-ing at environmental temperatures near or above 100 C, has revolutionized our ideas about the upper limit of temperature at which life can exist. | IFEBS Journal MINIREVIEW SERIES Protein hyperthermostability - current status and beyond Sotirios Koutsopoulos Center for BiomedicalEngineering Massachusetts Institute of Technology Cambridge MA USA The discovery of hyperthermophilic microorganisms thriving at environmental temperatures near or above 100 C has revolutionized our ideas about the upper limit of temperature at which life can exist. The characterization of hyperthermostable proteins has broadened our understanding and presented new opportunities for solving one of the most challenging problems in biophysics how is structural stability and biological function retained at high temperatures where normal proteins undergo dramatic structural changes The general consensus has been that protein hyperthermostability does not involve any aberrant features but rather is accomplished through modifying only the distribution of structural features . extended ion pair networks increased packing density decreased number of surface loops prevalence of specific amino acids in the sequence etc. that stabilize proteins which are adjusted to other environmental conditions. This series contains four articles encompassing different approaches to and aspects of protein hyperthermostability. In the first article Matsui and Harata analyze crystallographic data from homologous mesophilic thermophilic and hyperthermophilic proteins and discuss the importance of buried polar interactions. It has been long suggested that ion pair interactions are essential to stabilize the protein structure at high temperatures. Herein it is proposed that ion pairs in the core are more important than those on the surface of hyperthermostable proteins. In the second review Luke and colleagues carefully distinguish between hyper-thermophilic and thermophilic proteins and compare them with their mesophilic counterparts. Thermodynamic and kinetic data of protein unfolding in vitro reveal remarkable differences the study concludes that .

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