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Showing papers on "Protein–protein interaction published in 1980"


BookDOI
01 Jan 1980
TL;DR: A molecular approach to Immunity and Pathogenicity in an Insect-Bacterial System, and a Molecular Mechanism of Protein Biosynthesis and an approach to the mechanism of Energy Transduction.
Abstract: A Recognition of Ligands - Enzymic Catalysis- 1 What Everyone Wanted to Know About Tight Binding and Enzyme Catalysis, but Never Thought of Asking- 2 The Cytochromes c: Paradigms for Chemical Recognition- 3 Recognition of Ligands by Haem Proteins- 4 Influences of Solvent Water on the Transition State Affinity of Enzymes, Protein Folding, and the Composition of the Genetic Code- 5 Suicide Substrates: Mechanism-Based Inactivators of Specific Target Enzymes- 6 Recognition: the Kinetic Concepts- 7 Coupled Oscillator Theory of Enzyme Action- 8 Stereochemical Aspects of Chain Lengthening and Cyclization Processes in Terpenoid Biosynthesis- B Enzyme Regulation- 1 Three Multifunctional Protein Kinase Systems in Transmembrane Control- 2 Effect of Catabolite Repression on Chemotaxis in Salmonella typhimurium- 3 Subunit Interaction of Adenylylated Glutamine Synthetase- 4 Dynamic Compartmentation- 5 The Genes for and Regulation of the Enzyme Activities of two Multifunctional Proteins Required for the De Novo Pathway for UMP Biosynthesis in Mammals- 6 Regulation of Muscle Contraction by Ca Ion- 7 Why is Phosphate so Useful?- 8 ppGpp, a Signal Molecule- 9 Gramicidin S-Synthetase: On the Structure of a Polyenzyme Template in Polypeptide Synthesis- 10 A Molecular Approach to Immunity and Pathogenicity in an Insect-Bacterial System- C Nucleic Acid - Protein Interactions Mutagenesis- 1 Structure of the Gene 5 DNA Binding Protein from Bacteriophage fd and its DNA Binding Cleft- 2 Recognition of Nucleic Acids and Chemically-Damaged DNA by Peptides and Proteins- 3 Specific Interaction of Base-Specific Nucleases with Nucleosides and Nucleotides- 4 Structural and Dynamic Aspects of Recognition Between tRNAs and Aminoacyl-tRNA Synthetases- 5 Recognition of Promoter Sequences by RNA Polymerases from Different Sources- 6 DNA as a Target for a Protein Antibiotic: Molecular Basis of Action- 7 Site-Specific Mutagenesis in the Analysis of a Viral Replicon- D Protein Biosynthesis- 1 Molecular Mechanism of Protein Biosynthesis and an Approach to the Mechanism of Energy Transduction- 2 On Codon - Anticodon Interactions- 3 Fluorescent tRNA Derivatives and Ribosome Recognition- 4 Structure and Evolution of Ribosomes- E Philosophical Reflexions- 1 Molecular Biology, Culture, and Society- 2 Personal Recollections of Fritz Lipmann During the Early Years of Coenzyme A Research

25 citations


Journal ArticleDOI
TL;DR: The sequence domains that contribute to the surfaces of contact between Troponin-C and the other regulatory protein subunits of skeletal muscle troponin are proposed on the basis of data obtained by proton magnetic resonance and other physicochemical studies on the interaction with Troponins I and its peptide fragments.

16 citations


Book ChapterDOI
01 Jan 1980
TL;DR: The number of parameters which potentially can alter protein structure—and thereby protein function—is greater for membrane-bound enzymes than for soluble enzymes, since particulate enzymes are likely to be in contact with or partially embedded in the hydrophobic portion of the membrane bilayer and exposed to an aqueous environment.
Abstract: Soluble enzymes have been shown to undergo changes in conformation which result in modification of their kinetic properties. These changes can result from alterations in the enzyme’s environment or from the binding of soluble ligands. Both of these well-known phenomena are useful for the dynamic regulation of rates of substrate flux in various metabolic pathways (Atkinson, 1966; Stadtman, 1966; Koshland, 1970). Interest in this type of regulatory mechanism has focused on the properties of soluble proteins and enzymes, but the same general principles are likely to apply also to proteins which are bound to membrane structures. In fact, the number of parameters which potentially can alter protein structure—and thereby protein function—is greater for membrane-bound enzymes than for soluble enzymes, since particulate enzymes are likely to be in contact with or partially embedded in the hydrophobic portion of the membrane bilayer and exposed to an aqueous environment (Singer and Nicolsen, 1972). Furthermore, besides the binding of soluble ligands, changes in the gross composition or structure of the lipid bilayer could alter the properties of proteins which interact with it.

7 citations