Book of Abstracts: Albany 2011
June 14-18 2011
©Adenine Press (2010)
Universality of the spatial distribution of the backbones and a narrow band of amino acid stoichiometries amidst the structural and functional diversity of folded proteins
Is there a universal principle guiding protein folding besides the thermodynamic hypothesis of Anfinsen? Rigorous analyses of several thousand crystal structures of folded proteins reveal a surprisingly simple unifying principle of backbone organization (1, 2). We find that protein folding is a direct consequence of a narrow band of stoichiometric occurrences of amino-acids in primary sequences, regardless of the size and the fold of the protein. Furthermore, the amino acid residues in folded proteins display novel and invariant neighborhoods, independent of their locations (e.g. center vs. periphery) in contrast to anticipations from preferential interaction theories (3). These findings present a compelling case for a newer view of protein folding which takes into account solvent mediated and amino acid shape and size assisted optimization of the tertiary structure of the polypeptide chain to make a functional protein.