Peptides as Probes in Muscle Research [Paperback]

Protein-protein interactions are involved in muscle contraction and signal transduction. This book describes how synthetic peptides may be used, much like antibodies, both as specific inhibitors and as molecular probes to explore the cognitive interfaces between interacting proteins and their functional significance. This offers the prospect of very selective intervention in cellular mechanisms. These timely contributions by several experts will appeal to the researchers in muscle physiology, cardiovascular pharmacology and cell biology who are interested in this new approach.Protein-protein interactions are involved in muscle contraction and signal transduction. This book describes how synthetic peptides may be used, much like antibodies, both as specific inhibitors and as molecular probes to explore the cognitive interfaces between interacting proteins and their functional significance. This offers the prospect of very selective intervention in cellular mechanisms. These timely contributions by several experts will appeal to the researchers in muscle physiology, cardiovascular pharmacology and cell biology who are interested in this new approach.Structure of Actin.- Interaction of Actin 128 with Myosin and Troponin I and the Importance of these Interactions to Muscle Regulation.- Probing Myosin Head Structures with Monoclonal Antibodies and Recombinant Technology.- An Actin-Binding Site on Myosin.- Competitive Inhibition of Maximum Ca-Activated Force in Skinned Muscle Fibers by Cationic Peptides from the SH-1 Region of Myosin Heavy Chain.- The Use of Peptide Mimetics to Define the Actin-Binding Sites on the Head of the Myosin Molecule.- Interference of Myosin Peptides with Weak and Strong Actin Interaction of Cross-Bridges in Skeletal Muscle Fibres.- Caldesmon Derived Polypeptides as Probes of Force Production in Skeletal Muscle.- Myosin and Troponin Peptides Affect Calcium Sensitivity of Skinned Muscle Fibres.- Peptides as Probes of the Mechanisms Regulating SmolÇ