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.
Prof. Dr. med., Ph. D., Johann Caspar Rüegg, geb. 1930 in Zürich. Medizinstudium in Zürich und Dissertation beim Hirnphysiologen und Nobelpreisträger W. R. Hess. 1955-59 Studium der Biochemie an der Universität Cambridge, Promotion zum Ph. D. Bis 1967 Wissenschaftlicher Assistent am Max-Planck-Institut für Medizinische Forschung; 1963 Habilitation für Physiologische Chemie an der Universität Heidelberg; 1964/65 Senior Research Officer an der Universität Oxford; 1967-73 Wissenschaftlicher Rat und Professor am Institut für Zellphysiologie der Ruhr-Universität Bochum. 1973-1998 Ordinarius und Leiter des 2. Physiologischen Instituts der Universität Heidelberg. 1974 Adolf-Fick-Preis für Verdienste in Physiologie. 1981 Gastprofessor, seit 1985 Adjunct Professor in Physiologie an der Universität Cincinnati (Ohio). Seit 1998 korrespondierendes Mitglied der Schweizerischen Akademie der Medizinischen Wissenschaften.
Inhaltsangabe
Structure of Actin.- Interaction of Actin 1-28 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 Smooth Muscle Contractility: Studies on Skinned Fibres.- Antibodies as Probes of the Mechanisms Regulating Smooth Muscle Contractility: Studies on Skinned Fibres.- Regulation of Ca2+ Release from Sarcoplasmic Reticulum of Skeletal Muscle by an Endogenous Substance.- Defining Sites and Mechanisms of Interaction Between Rhodopsin and Transducin.- Comparative Studies on Chicken Skeletal and Smooth Muscle Dystrophins.- Use of Synthetic Peptides in the Study of the Function of Dystrophin.
Structure of Actin.- Interaction of Actin 1-28 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 Smooth Muscle Contractility: Studies on Skinned Fibres.- Antibodies as Probes of the Mechanisms Regulating Smooth Muscle Contractility: Studies on Skinned Fibres.- Regulation of Ca2+ Release from Sarcoplasmic Reticulum of Skeletal Muscle by an Endogenous Substance.- Defining Sites and Mechanisms of Interaction Between Rhodopsin and Transducin.- Comparative Studies on Chicken Skeletal and Smooth Muscle Dystrophins.- Use of Synthetic Peptides in the Study of the Function of Dystrophin.
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