Role of weak interactions in thermal stability of proteins.
A database analysis was done to study the role of weak interactions such as CHcdots, three dots, centeredO, CHcdots, three dots, centeredPI(m) and NHcdots, three dots, centeredPI(m) in the thermal stability of proteins. The CHcdots, three dots, centeredO and CHcdots, three dots, centeredPI(m) interactions are more in the case of thermophilic proteins as compared to mesophiles. Amino acid analysis showed that hydrophobic amino acids like Val and Ile, and Cys contribute more to CHcdots, three dots, centeredO hydrogen bonds where as Pro and Gly contribute more to CHcdots, three dots, centeredPI(m) interactions. Though NHcdots, three dots, centeredPI(m) interactions are dominated by Lys and Arg in thermophiles and mesophiles, the Arg contribution is significantly higher in thermophiles. Interestingly, Glycine is a predominant contributor to all the weak interactions. The number of aromatic amino acids in the thermophiles is more and hence a large number of aromatic clusters were observed in this class. Thus, a cumulative effect of weak interactions seems to be important in thermal stability of proteins. The study also shows that introduction of Gly, Arg, Phe, Pro, and Tyr may enhance the thermal stability.
Ibrahim
B Syed
BS
Department of Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India.
Pattabhi
Vasantha
V
D000596:Amino Acids / Q000737:chemistry*; D001105:Archaea / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry*; D001665:Binding Sites; D030562:Databases, Protein; D004789:Enzyme Activation; D004795:Enzyme Stability; D007700:Kinetics; D011485:Protein Binding; D020539:Sequence Analysis, Protein / Q000379:methods*; D013696:Temperature
D000596:Amino Acids; D019843:Archaeal Proteins