Institute of Information Science, Academia Sinica

Abstract: The biological activity and functional specificity of proteins depend on their native three-dimensional structures, which are defined by the corresponding chemical compositions or sequences. Statistics on the structures suggests that, there are universal geometric factors as constraints on native conformations, while the combinations of properties of amino acids in sequences lead to diversity of functions. In this talk, I will introduce our recent works on structure, stability, and dynamics of biomolecules based on adaptive data analysis approaches which are developed to reconcile two concepts. Two case studies, including local hydrophobicity and secondary structure formations in staphylococcal nuclease, and salt-bridge dynamics in the mechanical folding of titin kinase, will be discussed.