Preface

Special issue on “Membrane Protein Dynamics: Correlating Structure to Function”

Gianluigi Veglia is an Associate Professor of Chemistry and Biochemistry at the University of Minnesota. He received his M.S. from the University of Rome, La Sapienza, with a thesis on the “Synthesis and NMR Characterization of New β-Carboline Derivatives” under the direction of Professors M.R. Del Giudice and M. Delfini. He received his Ph.D. in physical chemistry from the University of Rome, La Sapienza. His thesis focused on the study of “Macromolecular Interactions by NMR Spectroscopy” carried out in the laboratory of Professor M. Delfini. During this time, he also studied the dynamics of small peptides and molecules using molecular dynamics simulations in collaboration with Professor A. Di Nola. Veglia carried out his postdoctoral studies with Professor S. Opella in the Chemistry Department of the University of Pennsylvania, where he optimized solution NMR methods for the structure determination of membrane proteins. In 2000, he joined the Department of Chemistry at the University of Minnesota as an Assistant Professor, where he began his independent program on the structural and dynamic characterization of soluble and membrane-bound proteins responsible for muscle contractility. He was then promoted to Associate Professor with a joint appointment between the Department of Chemistry and the Department of Biochemistry, Molecular Biology & Biophysics. Dr. Veglia uses an interdisciplinary approach to study the structure, dynamics, and interactions of integral and peripheral membrane proteins. Specifically, he combines solution NMR, solid-state NMR, and computational methods into a hybrid approach to determine the high-resolution structures and dynamic movements of proteins in membranes. More details about Dr. Veglia’s research projects can be found at www.chem.umn.edu/groups/veglia/.

Professor Ayyalusamy Ramamoorthy obtained his Ph.D. in Chemistry in 1990 from the Indian Institute of Technology (Kanpur, India) working on the development of NQR spectroscopy. He subsequently moved to the Central Leather Research Institute (a national research laboratory in Madras/Chennai, India) as a Fellow Scientist to develop scalar coupling based NMR methods for structural studies using solution NMR spectroscopy. In 1992, he joined JEOL Ltd (Tokyo, Japan) as a Scientist in the laboratory of Professor Kuniaki Nagayama to develop recoupling techniques (including USEME and J-HOHAHA) for magic angle spinning NMR studies on biological solids. He then joined the Stanley Opella group (University of Pennsylvania, Philadelphia) in 1993 to further develop and apply solid-state NMR techniques (including PISEMA, PSEUDO and PISEMAMAT) for structural studies of membrane proteins. In 1996, he joined the University of Michigan in Ann Arbor where he currently holds a joint appointment as Professor in Biophysics and Department of Chemistry. His main research interests are on the development and applications of solid-state NMR spectroscopy to study the structure, dynamics and function of membrane protein complexes, amyloid peptides, antimicrobial peptides, nanomedicine, and bone. His recent research revealed atomic-level mechanisms of membrane permeation/disruption by antimicrobial peptides and amyloid peptides, and reported high-resolution structure of membrane proteins. More details about his current research can be found at www.umich.edu/~ramslab.