Solid-State NMR Analysis of Interface Flexibility in Pleomorphic Protein Assemblies

Abstract

The structural proteins of the human immunodeficiency virus are characterized by their capacity to self-assemble and restructure themselves during the infectivity cycle. To understand the structural mechanisms that drive these protein assemblies, novel methods have been developed for the elucidation of molecular structure and dynamics. In this presentation, I will describe solid-state nuclear magnetic resonance (NMR) spectroscopy experiments for the analysis of the mature and the immature protein lattices of HIV-1 at the atomic level, with emphasis on the interactions that stabilize self-assembly and the mechanisms that facilitate structural reorganization in the critical maturation step of the virus infectivity cycle. I will also describe the application of solution NMR spectroscopy to guide batch-crystallization of proteins for solid-state NMR analysis of conformation and flexibility, with emphasis in the interfaces that give rise to variable curvature in asymmetric protein lattices.