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Phage display of proteins has become an important tool for protein engineering. Over the past year, the versatility of the technology has expanded to include the development of DNA-binding proteins with novel specificities, energetics of protein folding and directed evolution of antibodies. In...
Three-dimensional structures are now available for several immunoglobulin binding domains from bacterial proteins A, G, and L. X-ray diffraction and NMR experiments on complexes of these domains with portions of immunoglobulins have revealed common structural themes used in these interactions....
The current libraries of amino acid sequences of membrane proteins are a valuable resource for the analysis of elements common to these proteins. Multiple-sequence alignment techniques and the identification of conserved features of transmembrane segments have improved the prediction of membrane...
Two recent X-ray structures shed new light on the molecular mechanisms by which viral proteins mediate membrane fusion. In both cases it is clear that the fusion proteins are capable of dramatic conformational rearrangements. Studies of the intracellular fusion machinery used in vesicular...
Current research into the morphology of lipid membranes focuses on three areas: first, the transformations and fluctuations of the shape of freely suspended vesicles; second, the morphology of membranes that experience mutual interactions or external forces arising, for example, from a...
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