A new model for protein stereospecificity
Article Abstract:
It has been possible to develop a model to explain the ability of proteins to discriminate between optical isomers on the basis of crystallographic data. It was established that the three-point attachment model for enzymes and drug receptors must be revised to provide a more general mechanism for stereospecificity. The new 'four-location' model does not require the presence of four binding sites. The model explains how D-isomers can occupy the three binding sites in an orientation that stops cleavage.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Crazy, but correct
Article Abstract:
Daniel E. Koshland Jr., an assistant professor at Brookhaven National Laboratory, New York, studied the mechanism for hexokinase activity based on Emil Fisher's long-established 'lock and key' theory for enzyme-substrate interactions that would result in catastrophic losses to side reactions in real life. He used template model, since water could not substitute for the larger glucose to induce a conformational change in the enzyme, allowing it to react.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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Prediction of the structure of a receptor-protein complex using a binary docking method
Article Abstract:
The binding sites of a maltose-binding protein (MBP) can be anticipated by a 'binary docking' method involving two MBP octapeptide sequences with mutations that prevent maltose chemotaxis. The peptides in the docked solution permit the construction of an MBP-receptor complex. The dependability of this technique gives it great promise in foreseeing protein-protein and peptide-protein interactions, a necessary step in drug design.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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