Titlebook: Specificity in Biological Interactions; Proceedings of a Wor C. Chagas,B. Pullman Conference proceedings 1984 Pontificia Academia Scientiar

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Theoretical Studies of Molecular Recognition and Catalysis by Enzymeseins, are summarized. It is then shown how application of this methodology to two enzyme-substrate systems (α-chymotrypsin plus oligopeptides and hen egg white lysozyme plus oligosaccharides) leads to computed binding modes and energies that agree with experiment. This agreement attests to the valid

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Flavouring

Structural Studies of DNA-Protein Interactions recognition sites on the DNA. One protein (Cro) is a repressor of gene expression, the second (CAP) usually stimulates gene expression and the third (λ repressor) can act as either a repressor or activator. The three proteins contain a substructure consisting of two consecutive α-helices that is vi

FACT

Protein-Nucleic Acid Interactions Models and Realityween individual amino acids and nucleotides or their constituents are hard to crystallize and even then, interactions are often not as expected. If nucleotides or single stranded polynucleotides bind to proteins, they unfold with torsion angle γ(O.,-C.,-C.,-C.,) in -. or . range instead of the usual

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Elements of Specific Recognition of Non-Intercalating Ligands in the Interaction with DNAThe elements involved in their specific binding with DNA double helix may be used in molecular interactions of biological systems. Two classes of DNA- binding drugs, netropsin-like oligopeptides and antitumour-active compounds having quarternary ammonium structures, are discussed as representative n