PDF《ProtDataTherm: A database for》

http://www.nserc-crsng.gc.ca/index_eng.asp. Competing interests: The authors have declared that no competing interests exist. microorganisms can help to approximate thermostability criteria of their expressed proteins and a direct relationship between the growth temperature of microorganisms and the melting point of their corresponding proteins [2]. Currently available data on homologous proteins are valuable for engineering of proteins to gain higher stability by for example introducing more salt-bridges or strengthening the hydrophobic cores within protein structure [3]. Although structure-based protein engineering, known as rational engineering or rational design, is the most popular methodology for thermostability engineering of proteins, the limited number of available protein structures is still a challenge to prevalent utilization of the methodology [4]. On the other hand, because of modern advances in DNA sequencing technologies, the number of sequenced proteins belonging to different families is growing rapidly [3, 5]. Advances in applications of protein sequences for protein engineering could assist the existing routine structure-based rational methods. The consensus concept (CC) is the most popular sequence- based protein engineering approach to extract thermo-stabilizing mutations out of homolo- gous sequences [6C17]. In CC approach, a multiple sequence alignment (MSA) is first made and then non-consensus residues are substituted by the most frequently occurring amino acids [5]. However, there is no guarantee that all suggested mutations induced by CC approach can increase thermostability [9, 14, 16, 18]. To detect thermo-stabilizing mutations with higher probability, one can take the advantage ........