Debbie Marks, HMS Systems Biology, Protein structure and function from sequences
Harvard Medical School, Department of Systems Biology
Amino acid covariation in proteins, extracted from the evolutionary sequence record, can be used to fold proteins, including transmembrane proteins. Addressing a fundamental challenge in computational molecular biology, a new prediction method (EVfold) applies a maximum entropy approach to infer evolutionary couplings between sequence positions from correlated mutations in the multiple sequence alignment of a protein family. When translated to distance constraints, such residue-residue couplings are sufficient to generate good all-atom models of proteins from different fold classes, ranging in size from 50 to more than 500 residues. We use the technique to predict previously unknown 3D structures of large transmembrane proteins of biomedical interest, from their sequences alone. We show how the method can also plausibly predict oligomerization, functional sites, and conformational changes.
Location: Carl Icahn Lab 200
Date/Time: 11/19/12 at 11:00 am - 11/19/12 at 12:00 pm
Category: Special Seminars
Department: Lewis-Sigler Institute
