I have been involved in structural studies on muscle proteins since 1969, starting as a postdoctoral fellow contributing to the original protein sequencing of actin and myosin. I did the original sequencing of troponin C and myosin light chains, showed that these proteins are homologous, and published accurate predictions of their three-dimensional structures. Subsequently, a total of more than twenty additional muscle and calcium-binding proteins from various sources were sequenced in my laboratory. These comparative studies helped to identify conserved regions with essential common functions and differences related to variations in their properties. More recently, I have applied the general protein and peptide chemistry techniques used in protein sequencing to other approaches such as chemical crosslinking and fluorescent probes. I have also shared my protein chemistry and sequencing expertise with many others in muscle and related fields over the years. My laboratory also expanded its experimental repertoire with new approaches for studying the structure and function of muscle proteins. We developed independent expertise in cloning, mutagenesis, DNA sequencing and expression of muscle proteins, purification of both natural and recombinant proteins, as well as various methods for testing the functional viability of natural, recombinant, mutated and chemically modified proteins. My major long-term research interest through the years has been to elucidate the molecular mechanism of calcium regulation of skeletal muscle contraction. I have recently begun to use modern methods of bioinformatics to investigate the structural, functional and evolutionary relationships among these and other muscle and muscle-related proteins.