Catalysis Meeting
A Catalysis Meeting is proposed that will bring together people from the molecular evolution community interested in models of sequence evolution with people from the protein structure/biophysical chemistry community interested in models of protein folding, interaction, and dynamics. The meeting is designed to be synthetic as there is increasing overlap in interest between these two groups. On the one hand, evolution provides information on sequences that nature has selected to function based upon folding into a given structure. On the other hand, structure and binding interactions provide important constraints on sequence evolution that lead to non-random substitution patterns. Further, the bioinformatic concept of function is evolving from an arbitrary term that is transferred by homology when a genome is annotated to a biophysical (quantitative) description of interactions and constraints as the era of systems biology emerges. This will ultimately enable the possibility of understanding the molecular evolution of species and their proteomes on a whole new level.
Modeling protein structural and energetic constraints on sequence evolution
| PI(s): | David Liberles (University of Wyoming) Sarah Teichmann (Cambridge University) |
| Start Date: | 1-May-2011 |
| End Date: | 30-Apr-2012 |
| Keywords: | gene structure and function, genomics, evolutionary genetics, mathematical modeling, molecular biology |
A Catalysis Meeting is proposed that will bring together people from the molecular evolution community interested in models of sequence evolution with people from the protein structure/biophysical chemistry community interested in models of protein folding, interaction, and dynamics. The meeting is designed to be synthetic as there is increasing overlap in interest between these two groups. On the one hand, evolution provides information on sequences that nature has selected to function based upon folding into a given structure. On the other hand, structure and binding interactions provide important constraints on sequence evolution that lead to non-random substitution patterns. Further, the bioinformatic concept of function is evolving from an arbitrary term that is transferred by homology when a genome is annotated to a biophysical (quantitative) description of interactions and constraints as the era of systems biology emerges. This will ultimately enable the possibility of understanding the molecular evolution of species and their proteomes on a whole new level.
Related products
Publications- The Interface of Protein Structure, Protein Biophysics, and Molecular Evolution Liberles, DA, Teichmann, S, Bahar I, Bastolla U, Bloom J, Bornberg-Bauer E, Colwell LJ, de Koning APJ, Dokholyan NV, Echave J, Elofsson A, Gerloff DL, Goldstein RA, Grahnen JA, Holder M, Lakner C, Lartillot N, Lovell S, Naylor G, Perica T, Pollock DD, Pupko T, Regan L, Roger A, Rubinstein N, Shakhnovich E, Sjolander E, Sunyaev S, Teufel AI, Thorne JL, Thornton JW, Weinreich DM, Whelan S. 2012. The Interface of Protein Structure, Protein Biophysics, and Molecular Evolution. Protein Science, in press.
