Titlebook: Aspartic Proteinases; Retroviral and Cellu Michael N. G. James Book 1998 The Editor(s) (if applicable) and The Author(s), under exclusive l

Corporeal

X-Ray Crystallographic Studies of the Structure-Function Relationships of HIV-1 Protease and enzymes for the mature virus. Hence, it is essential for the maturation and infectivity of the virus and is thus a major target for the development of inhibitor drugs. But these efforts have been handicapped by the development of drug resistant viral strains.

ESO

Optimization of a Macromolecular Inhibitor of HIV-1 Proteaseave been developed. However, there are numerous ways in which a drug can lose effectiveness during long-term therapy. In particular several protease-mediated mechanisms result in reduced antiviral sensitivity of the various anti HIV protease inhibitors. As with inhibitors of reverse transcriptase, p

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B-cell

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Investigation of an Allosteric Site of HIV-1 Proteinase Involved in Inhibition by Cu2+gands can interfere with their catalytic properties. The viral proteinase is responsible for processing of viral polyproteins and is essential for viral particle maturation. Inhibition of the proteinase is therefore an efficient means of preventing viral replication, a principle that is used by the

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opprobrious

Mechanism of Action of Aspartic Proteasesspective specific substrates produce in every case practically identical unstable electronic systems which include catalytic groups of the active center, a cleaved peptide bond and a water molecule. The idea of a similar mutual orientation of these components in all nonbonded complexes of aspartic p

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Theory and Method of a Priori Computation of Catalytic Acts of Aspartic and Serine Proteinases, that dynamic conformational properties of a polypeptide chain, manifesting in the folding process cannot be described using current ideas of classical equilibrium thermodynamics. Novel principles of non-linear nonequilibrium thermodynamics (Prigogine physics) have been introduced, giving for the f