Directed enzyme evolution, screening and selection method by Frances H. Arnold, George Georgiou

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By Frances H. Arnold, George Georgiou

California Institute of expertise, Pasadena. textual content provides experimental protocols for the iteration of molecular range. contains reproducible equipment for random mutagenesis of genes, for homologous and nonhomologous recombination, and for developing in vivo libraries in micro organism. For researchers.

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Chem Rev 24:253–70. Flores TP, Moss DM, Thornton JM (1994): An algorithm for automatically generating protein topology cartoons. Protein Eng 7:31–7. Fruton JS (1972): Molecules and Life: Historical Essays on the Interplay of Chemistry and Biology. New York: Wiley-Interscience. ] Gerhart JC, Pardee AB (1962): The enzymology of control by feedback inhibition. J Biol Chem 237:891–6. Govindarajan S, Goldstein RA (1996): Why are some protein structures so common? Proc Natl Acad Sci USA 93:3341–5. Govindarajan S, Recabarren R, Goldstein RA (1999): Estimating the total number of protein folds.

1). Structural Classification of Folds As more and more protein structures have been determined, development of increasingly specific fold classifications has become possible. Cyrus Chothia and Michael Levitt derived one of the first such classifications, which grouped proteins based on their predominant secondary structural element (Levitt and Chothia, 1976). This classification consisted of four groups: all α, all β, α/β, and α + β. All α proteins, as the name suggests, are based almost entirely on α helical structure, and all β structures are based almost entirely on β sheet.

5 Some proteins do not have an intrinsically ordered structure, but rather spend much of their time in a disordered state. Often, the function of these proteins depends on achieving an ordered structure only under certain conditions or while engaged in specific interactions (Wright and Dyson, 1999). THE TERTIARY STRUCTURE OF PROTEINS: THE GLOBAL THREE-DIMENSIONAL STRUCTURE The Protein Fold The final three-dimensional tertiary structure of a protein is commonly referred to as its fold. Appropriately, the process by which a linear polypeptide chain achieves its distinctive fold is known as protein folding.

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