مریم راشکی - ۱گروه تنوع زیستی، پژوهشکده علوم محیطی، پژوهشگاه علوم، تکنولوژی پیشرفته و علوم محیطی، دانشگاه تحصیلات تکمیلی صنعتی و فناوری پیشرفته، کرمان
مجتبی مرتضوی - ۲گروه بیوتکنولوژی، پژوهشکده علوم محیطی، پژوهشگاه علوم، تکنولوژی پیشرفته و علوم محیطی، دانشگاه تحصیلات تکمیلی صنعتی و فناوری پیشرفته، کرمان

To investigate transmembrane helixes in the protein structures of the seven cytochrome P450 enzymes for Beauveria bassiana, the TMHM (1) program; to detect signal peptides and other protease shear sites, the SignalP program (2); and to study some physical and chemical parameters of the examined proteins, the ProtParam program were used. The results showed that the number of transmembrane helixes in different sequences varied from 0 to 2. The CYP5337A1 and CYP52G11 did not have the helix and the CYP51F1 (yeast) and CYP53A2 had two helixes. In all cases (except CYP58), estimated amino acids of hellixes were greater than 18 and increased the probability of the transmembrane protein being present. In none of the analyzed sequences, peptide signal was detected. The shear region in different sequences was located between positions 14-31 to 17-39. The molecular weight of proteins was calculated between 57,000 and 64,000. Also, the results showed that only the CYP539B5 and CYP52G11 proteins were stable. The CYP584Q1 and CYP617N1 had the highest and lowest amount of hydrophilic amino acids, respectively. The highest and lowest aliphatic indexes were related to the CYP617N1 and CYP52X1, respectively, that was directly related to the degree of heat tolerance.

Beauveria bassiana, Cytochrome P450, helix, peptide signal, software