Overcoming the Key Challenges in De Novo Protein Design: Enhancing Computational Efficiency and Incorporating True Backbone Flexibility.

Autor: Hearn, Donald W., Mondaini, Rubem P., Pardalos, Panos M., Floudas, Christodoulos A., Fung, Ho Ki, Morikis, Dimitrios, Taylor, Martin S., Zhang, Li
Zdroj: Mathematical Modelling of Biosystems; 2008, p133-183, 51p
Abstrakt: De novo protein design is initiated with a postulated or known flexible threedimensional protein structure and aims at identifying amino acid sequences compatible with such a structure. The problem was first denoted as the "inverse folding problem" [4, 5] since protein design has intimate links to the well-known protein folding problem [6]. While the protein folding problem aims at determining the single structure for a sequence, the de novo protein design problem exhibits a high level of degeneracy; that is, a large number of sequences are always found to share a common fold, although the sequences will vary with respect to properties such as activity and stability. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index