Modern research in biology increasingly relies on multiple techniques for describing structures and mechanisms. This book provides an overview of the contemporary integrated biology approaches for solving structures and understanding mechanisms of complex biological systems. It includes several methodology chapters discussing the current developments in the areas of cryo-electron microscopy (EM) and cryo-electron tomography (ET), computational biophysics, solution NMR spectroscopy, solid-state NMR spectroscopy and dynamic nuclear polarization (DNP), electron paramagnetic resonance (EPR), (photo-)chemically induced dynamic nuclear polarization (CIDNP), X-ray crystallography and small-angle X-ray and neutron scattering (SAXS/SANS). Several subsequent chapters demonstrate how these methods are used in synergy to address problems at the forefront of structural biology, with particular emphasis on examples where individual techniques are insufficient. Examples of biological systems include membrane proteins, viral protein assemblies, cytoskeleton protein assemblies, photosynthetic reaction centers, large enzyme complexes and whole cells.
The book is targeted to both the current practitioners of structural biology and scientists who are interested in entering the fields of structural biology or biophysical chemistry.
Angela Gronenborn is the head of the Department of Structural Biology at the University of Pittsburgh School of Medicine and the holder of the UPMC Rosalind Franklin Chair. She specializes in the use of NMR spectroscopy to study proteins and macromolecular complexes. Her work has focused on the study of proteins involved in human immunodeficiency virus (HIV) replication and she directs the Pittsburgh Center for HIV Protein Interactions.
Tatyana Polenova is a Professor of Chemistry and Biochemistry and the Director of an NIH Center of Biomedical Research Excellence (NIH-COBRE, "Molecular Design of Advanced Biomaterials"). Her research focuses on understanding structure, dynamics and function of biomolecular assemblies, using magnetic resonance and computational methods. She studies physiologically important microtubule/cargo protein assemblies whose malfunction is associated with multiple diseases, HIV-1 capsid protein assemblies whose function is important in virus pathogenicity and biotechnologically important vanadium haloperoxidases. Her research involves development of new NMR techniques.
Caitlin Quinn is an NMR Spectroscopist with the University of Delaware Nuclear Magnetic Resonance Core Facility. Her research focuses on applications of solid-state NMR to a wide range of biological, inorganic, and organic systems, with a particular interest in structure and dynamics of proteins associated with HIV-1 viral maturation and interactions with host factors. She is also interested in NMR methods development.
